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"thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Maxwell-Joyce-Bennett", "name": { "family": "Maxwell", "given": "Joyce Bennett" } } ] }, "title": "Part I. Synthesis of L-Arnino Acid Oxidase by a Serine- or Glycine-Requiring Strain of Neurospora. Part II. Studies Concerning Multiple Electrophoretic Forms of Tyrosinase in Neurospora", "ispublished": "unpub", "full_text_status": "public", "keywords": "(Genetics and Biochemistry)", "abstract": "
Part I: Synthesis of L-Amino Acid Oxidase by a Serine- or Glycine-Requiring\r\nStrain of Neurospora
\r\n\r\nWild-type cultures of Neurospora crassa growing on minimal\r\nmedium contain low levels of L-amino acid oxidase, tyrosinase, and\r\nnicotinarnide adenine dinucleotide glycohydrase (NADase). The enzymes\r\nare derepressed by starvation and by a number of other conditions which\r\nare inhibitory to growth. L-amino acid oxidase is, in addition, induced\r\nby growth on amino acids. A mutant which produces large quantities of\r\nboth L-amino acid oxidase and NADase when growing on minimal medium was\r\ninvestigated. Constitutive synthesis of L-amino acid oxidase was shown\r\nto be inherited as a single gene, called P110, which is separable from\r\nconstitutive synthesis of NADase. P110 maps near the centromere on\r\nlinkage group IV.
\r\n\r\nL-amino acid oxidase produced constitutively by P110 was partially\r\npurified and compared to partially purified L-amino acid oxidase\r\nproduced by derepressed wild-type cultures. The enzymes are identical\r\nwith respect to thermostability and molecular weight as judged by gel\r\nfiltration.
\r\n\r\nThe mutant P110 was shown to be an incompletely blocked auxotroph\r\nwhich requires serine or glycine. None of the enzymes involved\r\nin the synthesis of serine from 3-phosphoglyceric acid or glyceric acid\r\nwas found to be deficient in the mutant, however. An investigation of\r\nthe free intracellular amino acid pools of P110 indicated that the\r\nmutant is deficient in serine, glycine, and alanine, and accumulates\r\nthreonine and homoserine.
\r\n\r\nThe relationship between the amino acid requirement of P110 and\r\nits synthesis of L-amino acid oxidase is discussed.
\r\n\r\nPart II: Studies Concerning Multiple Electrophoretic Forms of Tyrosinase\r\nin Neurospora
\r\n\r\nSupernumerary bands shown by some crude tyrosinase preparations\r\nin paper electrophoresis were investigated. Genetic analysis indicated\r\nthat the location of the extra bands is determined by the particular T\r\nallele present. The presence of supernumerary bands varies with the\r\nmethod used to derepress tyrosinase production, and with the duration\r\nof derepression. The extra bands are unstable and may convert to the\r\nmajor electrophoretic band, suggesting that they result from modification\r\nof a single protein. Attempts to isolate the supernumerary bands\r\nby continuous flow paper electrophoresis or density gradient zonal\r\nelectrophoresis were unsuccessful.
", "date": "1970", "date_type": "degree", "id_number": "CaltechTHESIS:08132015-083412760", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechTHESIS:08132015-083412760", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Woodrow Wilson Foundation" }, { "agency": "Mayr Foundation" }, { "agency": "Public Health Service" } ] }, "collection": "CaltechTHESIS", "reviewer": "Tony Diaz", "deposited_by": "Benjamin Perez", "deposited_on": "2015-08-13 22:08:00", "doi": "10.7907/GHCK-W396", "alt_title": { "items": [ "Synthesis of L-Arnino Acid Oxidase by a Serine- or Glycine-Requiring Strain of Neurospora", "Studies Concerning Multiple Electrophoretic Forms of Tyrosinase in Neurospora" ] }, "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_defense_date": "1969-09-15", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "copyright_statement": "Author's Rights Authorization: I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted here is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive license to archive and make accessible, under the conditions specified under \"Thesis Availability\" in this submission, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation, or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1970", "author_list": "Maxwell, Joyce Bennett", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/10112", "eprint_id": 10112, "rev_number": 16, "documents": [ { "id": "/id/document/77276", "doc_id": 77276, "rev_number": 2, "files": [ { "id": "/id/file/218802", "fileid": 218802, "datasetid": "document", "objectid": 77276, "filename": "Shearn_AD_1969.pdf", "mime_type": "application/pdf", "hash": "d0aa2e39bb259a844118f8b770837cfa", "hash_type": "MD5", "filesize": 30308216, "mtime": "2017-03-28 21:38:00", "url": "/10112/1/Shearn_AD_1969.pdf" } ], "eprint_id": 10112, "pos": 1, "placement": 1, "mime_type": "application/pdf", "format": "application/pdf", "language": "en", "security": "public", "license": "other", "main": 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"/id/document/77276" }, { "type": "http://eprints.org/relation/isIndexCodesVersionOf", "uri": "/id/document/77276" } ] } } ], "eprint_status": "archive", "userid": 87, "dir": "disk0/00/01/01/12", "datestamp": "2017-03-29 14:25:23", "lastmod": "2022-11-09 19:20:20", "status_changed": "2017-03-29 14:25:23", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Shearn-Allen-David", "name": { "family": "Shearn", "given": "Allen David" } } ] }, "title": "A Study of the Possible Role of Transfer RNA in the Regulation of Enzyme Synthesis in Neurospora", "ispublished": "unpub", "full_text_status": "public", "keywords": "Biology", "abstract": "In several organisms, developmental transitions are accompanied\r\nby transfer RNA (tRNA) alterations. These alterations are usually\r\nobserved in the chromatographic profile of amino acyl-tRNA specific\r\nfor one or more amino acids and are of interest because of their possible\r\nsignificance in the regulation, at the translation level, of\r\nspecific protein synthesis and cell differentiation. I have investigated\r\nwhether such alterations accompany the biochemical differentiation of\r\nvegetative cultures of Neurspora crassa which occurs in response to\r\n\"hard-times,\" e.g., starvation or inhibition by amino acid analogs or\r\ncycloheximide. The synthesis of tyrosinase is a well-known characteristic\r\nof this developmental transition.
\r\n\r\n\r\nAfter determining the conditions required for the complete\r\ncharging of all 20 amino acids to Neurospora tRNA, I compared the\r\nchromatographic profile on methylated albumin-Kieselguhr columns of\r\namino acyl-tRNA's from vegetative cultures to those of cultures which\r\nwere derepressed for tyrosinase with ethionine, a methionine analog.\r\nNo qualitative tRNA alterations were observed; the same number of\r\ncomponents for each amino acid were found in cultures of both developmental\r\nstates and they had the same chromatographic mobilities.\r\nHowever, quantitative changes of acceptor activity were observed for\r\nseveral amino acids. The time course of the pattern of quantitative\r\nalteration suggests that the observed changes result from partial ribonuclease\r\ndigestion of the tRNA complement. I believe this ribonuclease\r\nis synthesized in response to the deprived environment and its function\r\nis to hydrolyze the RNA which is present in excess, in order that the\r\ncatabolic products may be used as building blocks for the synthesis\r\nof other kinds of molecules.
", "date": "1969", "date_type": "degree", "id_number": "CaltechTHESIS:03282017-143303527", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechTHESIS:03282017-143303527", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Public Health Service" } ] }, "collection": "CaltechTHESIS", "reviewer": "Tony Diaz", "deposited_by": "Benjamin Perez", "deposited_on": "2017-03-29 14:25:23", "doi": "10.7907/9TVD-N609", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_defense_date": "1968-07-10", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "copyright_statement": "Author's Rights Authorization: I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted here is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive license to archive and make accessible, under the conditions specified under \"Thesis Availability\" in this submission, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation, or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1969", "author_list": "Shearn, Allen David", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/10251", "eprint_id": 10251, "rev_number": 17, "documents": [ { "id": "/id/document/79344", "doc_id": 79344, "rev_number": 3, "files": [ { "id": "/id/file/224682", "fileid": 224682, "datasetid": "document", "objectid": 79344, "filename": "Logan_JB_1969.pdf", "mime_type": "application/pdf", "hash": "a328bd2dbca829258ed4dc05ad072ac9", "hash_type": "MD5", "filesize": 33602109, "mtime": "2017-06-02 16:02:54", "url": "/10251/1/Logan_JB_1969.pdf" } ], "eprint_id": 10251, "pos": 1, "placement": 1, "mime_type": "application/pdf", "format": "application/pdf", "language": "en", "security": "public", "license": "other", "main": 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"media_sample_start": "0", "media_sample_stop": "0", "content": "final" }, { "id": "/id/document/133649", "doc_id": 133649, "rev_number": 1, "files": [ { "id": "/id/file/379094", "fileid": 379094, "datasetid": "document", "objectid": 133649, "filename": "indexcodes.txt", "mime_type": "text/plain", "hash": "fa144ecb0b14801f08159fabd04bec93", "hash_type": "MD5", "filesize": 23181, "mtime": "2021-06-24 20:05:54", "url": "/10251/8/indexcodes.txt" } ], "eprint_id": 10251, "pos": 8, "placement": 8, "mime_type": "text/plain", "format": "other", "format_desc": "Generate index codes conversion from application/pdf to indexcodes", "language": "en", "security": "public", "license": "other", "main": "indexcodes.txt", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "relation": { "items": [ { "type": "http://eprints.org/relation/isVersionOf", "uri": "/id/document/79344" }, { "type": "http://eprints.org/relation/isVolatileVersionOf", "uri": "/id/document/79344" }, { "type": "http://eprints.org/relation/isIndexCodesVersionOf", "uri": "/id/document/79344" } ] } } ], "eprint_status": "archive", "userid": 87, "dir": "disk0/00/01/02/51", "datestamp": "2017-06-02 17:12:20", "lastmod": "2021-04-16 22:26:26", "status_changed": "2017-06-02 17:12:20", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Logan-James-Barrie", "name": { "family": "Logan", "given": "James Barrie" } } ] }, "title": "Biochemistry and Genetics of Canavanine Resistance in Neurospora", "ispublished": "unpub", "full_text_status": "public", "keywords": "Biochemistry", "abstract": "The pattern of inheritance of resistance to growth inhibition\r\nby canavanine in Neurospora crassa is shown to result from interactions\r\nbetween a major gene and several modifiers. The major gene controls\r\nthe production of a constitutive enzyme that destroys canavanine. The\r\nmodifiers affect the rate of uptake of the analog from the medium.\r\nStrains which lack the enzyme activity are canavanine sensitive; strains\r\nwhich possess it are resistant, but the level of resistance is dependent\r\non the rate of uptake.
\r\n\r\n\r\nThe canavanine degrading enzyme was partially purified and its\r\nproperties studied. The detoxification reaction was shown to be a\r\ncleavage of canavanine yielding hydroxyguanidine.
", "date": "1969", "date_type": "degree", "id_number": "CaltechTHESIS:06022017-085722120", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechTHESIS:06022017-085722120", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NSF" }, { "agency": "United States Public Health Service" } ] }, "collection": "CaltechTHESIS", "reviewer": "Tony Diaz", "deposited_by": "Benjamin Perez", "deposited_on": "2017-06-02 17:12:20", "doi": "10.7907/2j3p-es09", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_defense_date": "1969-02-24", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "copyright_statement": "Author's Rights Authorization: I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted here is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive license to archive and make accessible, under the conditions specified under \"Thesis Availability\" in this submission, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation, or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1969", "author_list": "Logan, James Barrie", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/10822", "eprint_id": 10822, "rev_number": 17, "documents": [ { "id": "/id/document/87842", "doc_id": 87842, "rev_number": 2, "files": [ { "id": "/id/file/249304", "fileid": 249304, "datasetid": "document", "objectid": 87842, "filename": "Pall_ML_1968.pdf", "mime_type": "application/pdf", "hash": "e0387a75e0ea36d84ff5bbe39cfa28e8", "hash_type": "MD5", "filesize": 33496836, "mtime": "2018-04-20 17:26:02", "url": "/10822/1/Pall_ML_1968.pdf" } ], "eprint_id": 10822, "pos": 1, "placement": 1, "mime_type": "application/pdf", "format": "application/pdf", "language": "en", "security": "public", "license": "other", "main": "Pall_ML_1968.pdf", 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"media_sample_start": "0", "media_sample_stop": "0", "content": "final" }, { "id": "/id/document/132776", "doc_id": 132776, "rev_number": 1, "files": [ { "id": "/id/file/378221", "fileid": 378221, "datasetid": "document", "objectid": 132776, "filename": "indexcodes.txt", "mime_type": "text/x-c", "hash": "f65382e2118f806df73a1ba1f0367cfe", "hash_type": "MD5", "filesize": 17517, "mtime": "2021-06-24 19:16:56", "url": "/10822/8/indexcodes.txt" } ], "eprint_id": 10822, "pos": 8, "placement": 8, "mime_type": "text/x-c", "format": "other", "format_desc": "Generate index codes conversion from application/pdf to indexcodes", "language": "en", "security": "public", "license": "other", "main": "indexcodes.txt", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "relation": { "items": [ { "type": "http://eprints.org/relation/isVersionOf", "uri": "/id/document/87842" }, { "type": "http://eprints.org/relation/isVolatileVersionOf", "uri": "/id/document/87842" }, { "type": "http://eprints.org/relation/isIndexCodesVersionOf", "uri": "/id/document/87842" } ] } } ], "eprint_status": "archive", "userid": 87, "dir": "disk0/00/01/08/22", "datestamp": "2018-04-20 20:02:46", "lastmod": "2019-12-21 02:58:38", "status_changed": "2018-04-20 20:02:46", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pall-Martin-Lawrence", "name": { "family": "Pall", "given": "Martin Lawrence" } } ] }, "title": "Part I. Tyrosinase Induction by Antimetabolites in Neurospora. Part II. Amino Acid Transport in Neurospora", "ispublished": "unpub", "full_text_status": "public", "keywords": "Biology; Biochemistry; Genetics", "abstract": "Part I.
\r\n\r\nA technique for inducing very high levels of tyrosinase activity \r\nwith various antimetabol ites is described. A modification of this tech\u00adnique \r\nwas used for studying tyrosinase induction in Neurospora over\r\nperiods of a few hours. An amount of the antimetabolite inducer \r\nsufficient to induce the enzyme is rapidly taken up into the mycelium. \r\nFollowing uptake, however, there is a lag period of about two hours \r\nbefore tyrosi nase is synthesized. During the lag period, some active, \r\nenergy requiring process prepares the mycelium for tyrosinase synthesis. \r\nRapid synthesis of tyrosinase then ensues. High concentrations of \r\ncycloheximide, an inhibitor of protein synthesis, inhibit the develop\u00adment \r\nof any further enzyme activity when added to inducing cultures, \r\nindicating that the synthesis of tyrosinase is de novo.
\r\n\r\nLow concentrations of cycloheximide which had been previously \r\nshown to induce tyrosinase, partially inhibit general protein synthesis.\r\nEthionine and parafluorophenyl alanine appear to induce the enzyme \r\nby being incorporated into proteins in place of methionine and phenylala\u00adnine, \r\nthus lowering the functional activity of newly synthesized\r\nproteins. The partial inhibition of the synthesis of functional \r\nproteins, then, is sufficient, in some way, to induce tyrosinase.
\r\n\r\nPart II.
\r\n\r\nKinetic studies have revealed the existence of two transport sys\u00adtems \r\nfor amino acids in Neurospora. Transport system I corresponds to \r\na system previously studied by Wiley and Matchett (24). Its activity \r\nis specifically missing in mtr mutant cultures previously described \r\nby Lester (26) and Stadler (25). It is capable of transporting most\r\nneutral L-amino acids. Amino acid transport system II has not been described \r\npreviously. It has an affinity for a wide variety of amino acids. It \r\ntransports amino acids with hydrophobic and hydrophilic side\r\nchains, both basic and neutral amino acids, and D- as well as L-amino \r\nacids. Transport system II has an affinity for both \u03b2- and \u03b1-amino \r\nacids.
\r\n\r\nTransport system I has high activity in young, rapidly growing cultures. \r\nTransport system II has little or no activity in young cultures. In older, \r\ncarbon-starved cultures, however, it is more active than transport system I. \r\nThis, together with the high affinities it shows\r\nfor many amino acids, suggests that amino acid transport \r\nsystem II serves a scavenger function, removing from the \r\nmedium traces of exogen\u00adous amino acids.
\r\n\r\n\r\n\r\n", "date": "1968", "date_type": "degree", "id_number": "CaltechTHESIS:04202018-102319427", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechTHESIS:04202018-102319427", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "McCallum Fund" }, { "agency": "Nutrition Foundation" } ] }, "collection": "CaltechTHESIS", "reviewer": "Tony Diaz", "deposited_by": "Benjamin Perez", "deposited_on": "2018-04-20 20:02:46", "doi": "10.7907/3025-N696", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_defense_date": "1967-11-10", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "copyright_statement": "Author's Rights Authorization: I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted here is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive license to archive and make accessible, under the conditions specified under \"Thesis Availability\" in this submission, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation, or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1968", "author_list": "Pall, Martin Lawrence", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/9244", "eprint_id": 9244, "rev_number": 18, "documents": [ { "id": "/id/document/61753", "doc_id": 61753, "rev_number": 2, "files": [ { "id": "/id/file/172954", "fileid": 172954, "datasetid": "document", "objectid": 61753, "filename": "Urey_jc_1966.pdf", "mime_type": "application/pdf", "hash": "37cf82d714724d18b7118d0a60f4b8a0", "hash_type": "MD5", "filesize": 30422456, "mtime": "2015-10-26 15:58:57", "url": "/9244/1/Urey_jc_1966.pdf" } ], "eprint_id": 9244, "pos": 1, "placement": 1, "mime_type": "application/pdf", "format": "application/pdf", "language": "en", "security": "public", "license": "other", "main": "Urey_jc_1966.pdf", 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"http://eprints.org/relation/isIndexCodesVersionOf", "uri": "/id/document/61753" } ] } } ], "eprint_status": "archive", "userid": 10575, "dir": "disk0/00/00/92/44", "datestamp": "2015-10-27 16:25:15", "lastmod": "2024-03-08 20:21:55", "status_changed": "2015-10-27 16:25:15", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Urey-John-Clayton", "name": { "family": "Urey", "given": "John Clayton" }, "show_email": "NO" } ] }, "title": "Enzyme Induction in Neurospora crassa", "ispublished": "unpub", "full_text_status": "public", "keywords": "(Biochemistry and Genetics)", "abstract": "I. Studies on Nicotinamide Adenine Dinucleotide Glycohydrase (NADase)
\r\nNADase, like tyrosinase and L-amino acid oxidase, is not present in two day old cultures of wild type Neurospora, but it is coinduced with those two enzymes during starvation in phosphate buffer. The induction of NADase, like tyrosinase, is inhibited by puromycin. The induction of all three enzymes is inhibited by actinomycin D. These results suggest that NADase is synthesized de novo during induction as has been shown directly for tyrosinase. NADase induction differs in being inhibited by certain amino acids.
\r\nThe tyrosinaseless mutant ty-1 contains a non-dialyzable, heat labile inhibitor of NADase. A new mutant, P110A, synthesizes NADase and L-amino acid oxidase while growing. A second strain, pe, fl;cot, makes NADase while growing. Both strains can be induced to make the other enzymes. These two strains prove that the control of these three enzymes is divisible. The strain P110A makes NADase even when grown in the presence of Tween 80. The synthesis of both NADase and L-amino acid oxidase by P110A is suppressed by complete medium. The theory of control of the synthesis of the enzymes is discussed.
\r\nII. Studies with EDTA
\r\nNeurospora tyrosinase contains copper but, unlike other phenol oxidases, this copper has never been removed reversibly. It was thought that the apo-enzyme might be made in vivo in the absence of copper. Therefore cultures were treated with EDTA to remove copper before the enzyme was induced. Although no apo-tyrosinase was detected, new information on the induction process was obtained.
\r\nA treatment of Neurospora with 0.5% EDTA pH 7, inhibits the subsequent induction during starvation in phosphate buffer of tyrosinase, L-amino acid oxidase and NADase. The inhibition of tyrosinase and L-amino acid oxidase induction is completely reversed by adding 5 x 10-5M CaCl2, 5 x 10-4M CuSO4, and a mixture of L-amino acids (2 x 10-3M each) to the buffer. Tyrosinase induction is also fully restored by 5 x 10-4M CaCl2 and amino acids. As yet NADase has been only partially restored.
\r\nThe copper probably acts by sequestering EDTA left in the mycelium and may be replaced by nickel. The EDTA apparently removes some calcium from the mycelium, which the added calcium replaces. Magnesium cannot replace calcium. The amino acids probably replace endogenous amino acids lost to the buffer after the EDTA treatment.
\r\nThe EDTA treatment also increases permeability, thereby increasing the sensitivity of induction to inhibition by actinomycin D and allowing cell contents to be lost to the induction buffer. EDTA treatment also inhibits the uptake of exogenous amino acids and their incorporation into proteins.
\r\nThe lag period that precedes the first appearance of tyrosinase is demonstrated to be a separate dynamic phase of induction. It requires oxygen. It is inhibited by EDTA, but can be completed after EDTA treatment in the presence of 5 x 10-5M CaCl2 alone, although no tyrosinase is synthesized under these conditions.
\r\nThe time course of induction has an early exponential phase suggesting an autocatalytic mechanism of induction.
\r\nThe mode of action of EDTA, the process of induction and the kinetics of induction are discussed.
\r\n", "date": "1966", "date_type": "degree", "id_number": "CaltechTHESIS:10262015-082758473", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechTHESIS:10262015-082758473", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "U. S. Public Health Service", "grant_number": "2G-86" }, { "agency": "Woodrow Wilson Foundation" }, { "agency": "NSF" } ] }, "collection": "CaltechTHESIS", "reviewer": "Kathy Johnson", "deposited_on": "2015-10-27 16:25:15", "doi": "10.7907/MBMA-NM23", "divisions": { "items": [ "div_chem" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_defense_date": "1965-06-23", "review_status": "approved", "option_major": { "items": [ "bioch" ] }, "option_minor": { "items": [ "biology" ] }, "copyright_statement": "Author's Rights Authorization: I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted here is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive license to archive and make accessible, under the conditions specified under \"Thesis Availability\" in this submission, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation, or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1966", "author_list": "Urey, John Clayton", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/661", "eprint_id": 661, "rev_number": 10, "documents": [ { "id": "/id/document/976", "doc_id": 976, "rev_number": 2, "files": [ { "id": "/id/file/6160", "fileid": 6160, "datasetid": "document", "objectid": 976, "filename": "Sueoka_n_1959.pdf", "mime_type": "application/pdf", "filesize": 6462669, "mtime": "2012-12-26 02:31:17", "url": "/661/1/Sueoka_n_1959.pdf" } ], "eprint_id": 661, "pos": 1, "mime_type": "application/pdf", "format": "application/pdf", "format_desc": "Sueoka_n_1959.pdf", "language": "en", "security": "public", "license": "other", "main": "Sueoka_n_1959.pdf", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "content": "final", "relation": { "items": [ { "type": "http://eprints.org/relation/hasVolatileVersion", "uri": "/id/document/17778" }, { "type": "http://eprints.org/relation/haspreviewThumbnailVersion", "uri": "/id/document/17778" }, { "type": "http://eprints.org/relation/hasVersion", "uri": "/id/document/17778" } ] } }, { "id": "/id/document/17778", "doc_id": 17778, "rev_number": 2, "files": [ { "id": "/id/file/6158", "fileid": 6158, "datasetid": "document", "objectid": 17778, "filename": "preview.png", "mime_type": "image/png", "hash": "653c5ae24baaf91f85d06e32882e0fd5", "hash_type": "MD5", "filesize": 8816, "mtime": "2012-12-26 02:31:17", "url": "/661/2/preview.png" } ], "eprint_id": 661, "pos": 2, "placement": 2, "mime_type": "image/png", "format": "image/png", "language": "en", "security": "public", "license": "other", "main": "preview.png", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "relation": { "items": [ { "type": "http://eprints.org/relation/isVolatileVersionOf", "uri": "/id/document/976" }, { "type": "http://eprints.org/relation/ispreviewThumbnailVersionOf", "uri": "/id/document/976" }, { "type": "http://eprints.org/relation/isVersionOf", "uri": "/id/document/976" } ] } } ], "eprint_status": "archive", "userid": 2, "dir": "disk0/00/00/06/61", "datestamp": "2006-02-21", "lastmod": "2022-02-11 23:20:52", "status_changed": "2009-09-25 01:43:09", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Sueoka-Noburu", "name": { "family": "Sueoka", "given": "Noburu" }, "show_email": "NO" } ] }, "title": "Genetic and Biochemical Studies of Tyrosinase in Neurospora and Laccase in Neurospora", "ispublished": "unpub", "full_text_status": "public", "keywords": "(Genetics and Immunology)", "abstract": "NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document.\r\n\r\nPart I: Genetic and Biochemical Studies of Tyrosinase in Neurospora
\r\n\r\n1) A new form of tyrosinase of Neurospora crassa (Sing-2) was found, which has different electrophoretic behavior and thermostability from the three previously known forms ([...], [...] and [...]).
\r\n\r\n2) The characteristics of the new form are determined by the single locus, T, which also controls the characteristics of the other forms.
\r\n\r\n3) The kinetics of thermal inactivation of the different tyrosinases were studied in detail at different temperatures.
\r\n\r\n4) Two tyrosinaseless genes (ty-l and ty-2) are independent from each other and from the T-locus, and both of them are epistatic to the T-locus.
\r\n\r\n5) Heterocaryons of the following genotypes were produced. [...]. It was found that a) the ty-1 allele is recessive to its normal form, [...], b) Het.B and Het.D produce a mixture of both forms of tyrosinase determined by their genotypes, and c) the ratio of the two enzyme forms produced corresponds to the ratio of the two component nuclei in the heterocaryons.
\r\n\r\n6) The significance of the present findings for the gene-enzyme relationship is discussed.
\r\n\r\nPart II: Laccase in Neurospora
\r\n\r\nThe \"second phenol oxidase\" in Neurospora reported by Horowitz and Fling (1953) was further studied.
\r\n\r\n1) The enzyme was purified, characterized as to substrate specificity, inhibitor spectrum, and pH optimum, and identified as a laccase.
\r\n\r\n2) Production of laccase shows wide variability among different strains of Neurospora and is influenced greatly by external factors, such as temperature, concentrations of sulfur and copper of the medium.
\r\n\r\n3) Immunological studies show that there is no serological similarity between laccase and tyrosinase of Neurospora.
\r\n\r\n4) Inducibility of laccase in Neurospora is a variable character, but seems to be strain specific.
", "date": "1959", "date_type": "degree", "id_number": "CaltechETD:etd-02172006-105349", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechETD:etd-02172006-105349", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "collection": "CaltechTHESIS", "reviewer": "Kathy Johnson", "deposited_by": "Imported from ETD-db", "deposited_on": "2006-02-21", "doi": "10.7907/1G65-FS46", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_submitted_date": "2006-02-17", "thesis_defense_date": "1959-01-01", "thesis_approved_date": "2006-02-21", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "option_minor": { "items": [ "immun" ] }, "copyright_statement": "I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive\nlicense to archive and make accessible, under the conditions specified below,\nmy thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1959", "author_list": "Sueoka, Noburu", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/4924", "eprint_id": 4924, "rev_number": 9, "documents": [ { "id": "/id/document/7832", "doc_id": 7832, "rev_number": 2, "files": [ { "id": "/id/file/48131", "fileid": 48131, "datasetid": "document", "objectid": 7832, "filename": "Fischer_ga_1954.pdf", "mime_type": "application/pdf", "filesize": 3241465, "mtime": "2012-12-26 03:12:59", "url": "/4924/1/Fischer_ga_1954.pdf" } ], "eprint_id": 4924, "pos": 1, "mime_type": "application/pdf", "format": "application/pdf", "format_desc": "Fischer_ga_1954.pdf", "language": "en", "security": "public", "license": "other", "main": "Fischer_ga_1954.pdf", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "content": "final", "relation": { "items": [ { "type": "http://eprints.org/relation/hasVolatileVersion", "uri": "/id/document/24343" }, { "type": "http://eprints.org/relation/haspreviewThumbnailVersion", "uri": "/id/document/24343" }, { "type": "http://eprints.org/relation/hasVersion", "uri": "/id/document/24343" } ] } }, { "id": "/id/document/24343", "doc_id": 24343, "rev_number": 2, "files": [ { "id": "/id/file/48129", "fileid": 48129, "datasetid": "document", "objectid": 24343, "filename": "preview.png", "mime_type": "image/png", "hash": "f0b7d63ea04a139bf2b8cc528a0862ff", "hash_type": "MD5", "filesize": 11426, "mtime": "2012-12-26 03:12:59", "url": "/4924/2/preview.png" } ], "eprint_id": 4924, "pos": 2, "placement": 2, "mime_type": "image/png", "format": "image/png", "language": "en", "security": "public", "license": "other", "main": "preview.png", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "relation": { "items": [ { "type": "http://eprints.org/relation/isVolatileVersionOf", "uri": "/id/document/7832" }, { "type": "http://eprints.org/relation/ispreviewThumbnailVersionOf", "uri": "/id/document/7832" }, { "type": "http://eprints.org/relation/isVersionOf", "uri": "/id/document/7832" } ] } } ], "eprint_status": "archive", "userid": 2, "dir": "disk0/00/00/49/24", "datestamp": "2003-12-12", "lastmod": "2022-02-11 23:10:30", "status_changed": "2009-09-25 03:28:35", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Fischer-Glenn-Albert", "name": { "family": "Fischer", "given": "Glenn Albert" }, "show_email": "NO" } ] }, "title": "Genetic and Biochemical Studies of the Cystine-Methionine Series of Mutants in Neurospora crassa", "ispublished": "unpub", "full_text_status": "public", "keywords": "(Genetics and Biochemistry)", "abstract": "NOTE: Text or symbols not renderale in plain ASCII are indicated by [...]. Abstract is included in .pdf document.\r\n\r\n1. The following enzyme activities were studied in extracts of wild type and mutant Neurospora: [...]. Activity 2 was shown to be absent in a homocysteineless mutant and activity 3 was shown to be absent in a cystathionineless mutant. It was found that a suppressor, obtained by Giles, which causes these mutants to grow on minimal, returns enzyme activity to the mutants. Each activity is shown to be catalyzed by a different enzyme.\r\n\r\n2. Evidence is presented which indicates that a Neurospora cystathionineless mutant can synthesize cystathionine from methionine without the intervention of cysteine.\r\n\r\n3. Mutants which are blocked between thiosulfate and cysteine are shown to grow on elemental sulfur and H[subscript 2]S.", "date": "1954", "date_type": "degree", "id_number": "CaltechETD:etd-12102003-111246", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechETD:etd-12102003-111246", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "collection": "CaltechTHESIS", "reviewer": "Kathy Johnson", "deposited_by": "Imported from ETD-db", "deposited_on": "2003-12-12", "doi": "10.7907/FP61-BW75", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_submitted_date": "2003-12-10", "thesis_defense_date": "1954-01-01", "thesis_approved_date": "2003-12-12", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "option_minor": { "items": [ "bioch" ] }, "copyright_statement": "I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive\nlicense to archive and make accessible, under the conditions specified below,\nmy thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1954", "author_list": "Fischer, Glenn Albert", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/10489", "eprint_id": 10489, "rev_number": 18, "documents": [ { "id": "/id/document/83403", "doc_id": 83403, "rev_number": 2, "files": [ { "id": "/id/file/235891", "fileid": 235891, "datasetid": "document", "objectid": 83403, "filename": "Thayer_PS_1952.pdf", "mime_type": "application/pdf", "hash": "485f18ccf2beb8396eb335caa56c10ec", "hash_type": "MD5", "filesize": 40134566, "mtime": "2017-10-05 20:30:47", "url": "/10489/1/Thayer_PS_1952.pdf" } ], "eprint_id": 10489, "pos": 1, "placement": 1, "mime_type": "application/pdf", "format": "application/pdf", "language": "en", "security": "public", "license": "other", "main": 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"/id/document/83403" }, { "type": "http://eprints.org/relation/isIndexCodesVersionOf", "uri": "/id/document/83403" } ] } } ], "eprint_status": "archive", "userid": 87, "dir": "disk0/00/01/04/89", "datestamp": "2017-10-05 21:16:15", "lastmod": "2023-05-16 23:38:10", "status_changed": "2017-10-05 21:16:15", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Thayer-Philip-Standish", "name": { "family": "Thayer", "given": "Philip Standish" }, "show_email": "NO" } ] }, "title": "Studies on the L-Amino Acid Oxidase of Neurospora crassa", "ispublished": "unpub", "full_text_status": "public", "keywords": "Biology, (Biochemistry and Chemistry)", "abstract": "The L-amino acid oxidase of Neurospora is a \r\ngen\u00aderal amino acid oxidase attacking a wide range of L-amino \r\nacids at different rates. Activity of the enzyme is de\u00adpendent \r\non substrate concentration, oxygen tension and\r\npH. Different amino acids show different pH optima. \r\nActivity is significantly reduced by excess substrate, \r\nand competition is exhibited between mixed substrates.
\r\n\r\n\r\nL-oxidase production by mycelium is increased 4 to \r\n10 fold by biotin limitation. This effect is not produced \r\nby: changes in extractability of the enzyme; reduced level \r\nof growth; defective ammonia, aspartic acid, or riboflavin \r\nmetabolism; or production of an inhibitor of the enzyme.
\r\n\r\n\r\nThe enzyme is adaptively formed during growth in \r\nthe presence of substrate amino acids. Factors affecting \r\nthe degree of adaptation are biotin and substrate concen\u00adtrations, \r\npH and strain differences. Deadaptation is pro\u00adduced \r\nby excess biotin or the removal of substrate. The\r\nrelation of adaptation to the low biotin effect is discussed.
\r\n\r\n\r\nThe L-oxidase is involved in detoxification of cana\u00advanine. \r\nStrain differences in canavanine sensitivity are paralleled \r\nby certain qualitative differences in L-oxidase activity. \r\nCanavanine resistance is increased on low biotin. \r\nThe relation of these observations to canavanine sensiti\u00advity \r\nand its genetic control is discussed.
", "date": "1952", "date_type": "degree", "id_number": "CaltechTHESIS:10052017-132646189", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechTHESIS:10052017-132646189", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH" }, { "agency": "United States Public Health Service" } ] }, "collection": "CaltechTHESIS", "reviewer": "Kathy Johnson", "deposited_by": "Benjamin Perez", "deposited_on": "2017-10-05 21:16:15", "doi": "10.7907/JJN0-XC39", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_defense_date": "1952-01-01", "review_status": "approved", "option_major": { "items": [ "bioch" ] }, "option_minor": { "items": [ "chemistry" ] }, "copyright_statement": "Author's Rights Authorization: I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted here is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive license to archive and make accessible, under the conditions specified under \"Thesis Availability\" in this submission, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation, or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1952", "author_list": "Thayer, Philip Standish", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" }, { "id": "https://thesis.library.caltech.edu/id/eprint/2748", "eprint_id": 2748, "rev_number": 10, "documents": [ { "id": "/id/document/5059", "doc_id": 5059, "rev_number": 2, "files": [ { "id": "/id/file/29503", "fileid": 29503, "datasetid": "document", "objectid": 5059, "filename": "Shen_sc_1951.pdf", "mime_type": "application/pdf", "filesize": 2313458, "mtime": "2012-12-26 02:54:04", "url": "/2748/1/Shen_sc_1951.pdf" } ], "eprint_id": 2748, "pos": 1, "mime_type": "application/pdf", "format": "application/pdf", "format_desc": "Shen_sc_1951.pdf", "language": "en", "security": "public", "license": "other", "main": "Shen_sc_1951.pdf", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "content": "final", "relation": { "items": [ { "type": "http://eprints.org/relation/hasVolatileVersion", "uri": "/id/document/21609" }, { "type": "http://eprints.org/relation/haspreviewThumbnailVersion", "uri": "/id/document/21609" }, { "type": "http://eprints.org/relation/hasVersion", "uri": "/id/document/21609" } ] } }, { "id": "/id/document/21609", "doc_id": 21609, "rev_number": 2, "files": [ { "id": "/id/file/29501", "fileid": 29501, "datasetid": "document", "objectid": 21609, "filename": "preview.png", "mime_type": "image/png", "hash": "01a4adfe253ae8b20927e2462ceae688", "hash_type": "MD5", "filesize": 8963, "mtime": "2012-12-26 02:54:04", "url": "/2748/2/preview.png" } ], "eprint_id": 2748, "pos": 2, "placement": 2, "mime_type": "image/png", "format": "image/png", "language": "en", "security": "public", "license": "other", "main": "preview.png", "media_duration": "0", "media_aspect_ratio": "0", "media_sample_start": "0", "media_sample_stop": "0", "relation": { "items": [ { "type": "http://eprints.org/relation/isVolatileVersionOf", "uri": "/id/document/5059" }, { "type": "http://eprints.org/relation/ispreviewThumbnailVersionOf", "uri": "/id/document/5059" }, { "type": "http://eprints.org/relation/isVersionOf", "uri": "/id/document/5059" } ] } } ], "eprint_status": "archive", "userid": 2, "dir": "disk0/00/00/27/48", "datestamp": "2004-06-29", "lastmod": "2022-02-11 23:30:38", "status_changed": "2009-09-25 02:44:06", "type": "thesis", "metadata_visibility": "show", "creators": { "items": [ { "id": "Shen-San-Chiun", "name": { "family": "Shen", "given": "San-Chiun" }, "show_email": "NO" } ] }, "title": "Genetics and Biochemistry of the Cysteine-Tyrosine Relationship in Neurospora crassa", "ispublished": "unpub", "full_text_status": "public", "keywords": "(Genetics and Biochemistry)", "abstract": "NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document.\r\n\r\nMutant 84605 which was obtained from wild type Neurospora crassa following X-ray treatment differs from wild type by a single gene located 4.8 units from the centromere of the second chromosome.
\r\n\r\nAt 25 [degrees], the mutant requires both cysteine and tyrosine for normal growth. At 35[degrees] only cysteine is required. The block in cysteine synthesis is the step sulfite [...] thiosulfate.
\r\n\r\nHigh tyrosinase activity was found in the mutant grown at 25[degrees], but not when grown at 35[degrees]. Under the same conditions, wild type shows little or no tyrosinase activity.
\r\n\r\nThe addition of cysteine to the medium causes an inhibition of the growth of wild type, and at the same time a marked increase in the tyrosinase activity occurs. The inhibition can be overcome by adding tyrosine to the medium, or by culturing at 35[degrees].
\r\n\r\nIt is suggested that the tyrosine requirement is caused by the high tyrosinase activity and that the latter, in turn, is caused by the defect in sulfur metabolism.
\r\n\r\nTwo natural inhibitors of tyrosinase have been found in Neurospora.
\r\n\r\nA powerful inhibitor of the growth of wild type accumulates in cultures of the mutant.
\r\n\r\nExperiments designed to test whether sulfide can serve as a sulfur source for Neurospora indicate that sulfide is utilized slightly, if at all.
\r\n\r\nExperiments with a double mutant have indicated that the production of cysteine from methionine by Neurospora does not involve simple reversal of the step homocysteine [...] methionine.
", "date": "1951", "date_type": "degree", "id_number": "CaltechETD:etd-06282004-093704", "refereed": "FALSE", "official_url": "https://resolver.caltech.edu/CaltechETD:etd-06282004-093704", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "collection": "CaltechTHESIS", "reviewer": "Kathy Johnson", "deposited_by": "Imported from ETD-db", "deposited_on": "2004-06-29", "doi": "10.7907/BE55-1F07", "divisions": { "items": [ "div_biol" ] }, "institution": "California Institute of Technology", "thesis_type": "phd", "thesis_advisor": { "items": [ { "id": "Horowitz-N-H", "name": { "family": "Horowitz", "given": "Norman Harold" }, "role": "advisor" } ] }, "thesis_committee": { "items": [ { "name": { "family": "Unknown", "given": "Unknown" } } ] }, "thesis_degree": "PHD", "thesis_degree_grantor": "California Institute of Technology", "thesis_submitted_date": "2004-06-28", "thesis_approved_date": "2004-06-29", "review_status": "approved", "option_major": { "items": [ "biology" ] }, "option_minor": { "items": [ "bioch" ] }, "copyright_statement": "I hereby certify that, if appropriate, I have obtained a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee.\n\nI hereby grant to California Institute of Technology or its agents the non-exclusive\nlicense to archive and make accessible, under the conditions specified below,\nmy thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report.", "resource_type": "thesis", "pub_year": "1951", "author_list": "Shen, San-Chiun", "advisor_list": "Horowitz, Norman Harold", "comittee_list": "Unknown, Unknown" } ]