<h1>Schroeder, Walter Adolph</h1>
<h2>Article from <a href="https://authors.library.caltech.edu">CaltechAUTHORS</a></h2>
<ul>
<li>Margalit, Ruth and Kostić, Nenad M., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:MARpnas84">Preparation and characterization of pentaammineruthenium-(histidine-83)azurin: Thermodynamics of intramolecular electron transfer from ruthenium to copper</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 81; No. 20; 6554-6558; PMCID PMC391964; <a href="https://doi.org/10.1073/pnas.81.20.6554">10.1073/pnas.81.20.6554</a></li>
<li>DeSimone, Joseph and Schroeder, W. A., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:DESblo84">Speciation in the baboon and its relation to gamma-chain heterogeneity and to the response to induction of HbF by 5-azacytidine</a>; Blood; Vol. 63; No. 5; 1088-1095; <a href="https://doi.org/10.1182/blood.V63.5.1088.1088">10.1182/blood.V63.5.1088.1088</a></li>
<li>Yocom, Kathryn M. and Shelton, Joan B., el al. (1982) <a href="https://resolver.caltech.edu/CaltechAUTHORS:YOCpnas82">Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 79; No. 22; 7052-7055; PMCID PMC347273; <a href="https://doi.org/10.1073/pnas.79.22.7052">10.1073/pnas.79.22.7052</a></li>
<li>Ringelhann, B. and Acquaye, C. T. A., el al. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20201201-130559876">Homozygotes for the hereditary persistence of fetal hemoglobin: The ratio of ^Gγ to ^Aγ chains and biosynthetic studies</a>; Biochemical Genetics; Vol. 15; No. 11-12; 1083-1096; <a href="https://doi.org/10.1007/bf00484499">10.1007/bf00484499</a></li>
<li>Huisman, T. H. J. and Harris, H., el al. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20221004-680171300.22">The chemical heterogeneity of the fetal hemoglobin in normal newborn infants and in adults</a>; Molecular and cellular biochemistry; Vol. 17; No. 1; 45-55; <a href="https://doi.org/10.1007/bf01732554">10.1007/bf01732554</a></li>
<li>Schroeder, W. A. and Huisman, T. H. J., el al. (1968) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SCHRpnas68">Evidence for multiple structural genes for the γ chain of human fetal hemoglobin</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 60; No. 2; 537-544; PMCID PMC225081; <a href="https://doi.org/10.1073/pnas.60.2.537">10.1073/pnas.60.2.537</a></li>
<li>Jones, Richard T. and Schroeder, W. A. (1963) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053942">Chemical Characterization and Subunit Hybridization of Human Hemoglobin H and Associated Compounds</a>; Biochemistry; Vol. 2; No. 6; 1357-1367; <a href="https://doi.org/10.1021/bi00906a031">10.1021/bi00906a031</a></li>
<li>Schroeder, W. A. and Shelton, J. Roger, el al. (1963) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053839">The Amino Acid Sequence of the γ Chain of Human Fetal Hemoglobin</a>; Biochemistry; Vol. 2; No. 5; 992-1008; <a href="https://doi.org/10.1021/bi00905a016">10.1021/bi00905a016</a></li>
<li>Schroeder, W. A. and Jones, Richard T., el al. (1962) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053738">Chromatographic Separation of Peptides on Ion Exchange Resins. Separation of Peptides from Enzymatic Hydrolyzates of the α, β, and γ Chains of Human Hemoglobins</a>; Analytical Chemistry; Vol. 34; No. 12; 1570-1575; <a href="https://doi.org/10.1021/ac60192a018">10.1021/ac60192a018</a></li>
<li>Schnek, A. G. and Schroeder, W. A. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053652">The Relation between the Minor Components of Whole Normal Human Adult Hemoglobin as Isolated by Chromatography and Starch Block Electrophoresis</a>; Journal of the American Chemical Society; Vol. 83; No. 6; 1472-1478; <a href="https://doi.org/10.1021/ja01467a046">10.1021/ja01467a046</a></li>
<li>Shelton, J. Roger and Schroeder, W. A. (1960) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053564">Further N-Terminal Sequences in Human Hemoglobins A, S and F by Edman's Phenylthiohydantoin Method</a>; Journal of the American Chemical Society; Vol. 82; No. 13; 3342-3345; <a href="https://doi.org/10.1021/ja01498a028">10.1021/ja01498a028</a></li>
<li>Rhinesmith, Herbert S. and Schroeder, W. A., el al. (1957) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180725-111211357">A Quantitative Study of the Hydrolysis of Human Dinitrophenyl(DNP)globin: The Number and Kind of Polypeptide Chains in Normal Adult Human Hemoglobin</a>; Journal of the American Chemical Society; Vol. 79; No. 17; 4682-4686; <a href="https://doi.org/10.1021/ja01574a028">10.1021/ja01574a028</a></li>
<li>Rhinesmith, Herbert S. and Schroeder, W. A., el al. (1957) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180725-111211261">The N-Terminal Amino Acid Residues of Normal Adult Human Hemoglobin: A Quantitative Study of Certain Aspects of Sanger's DNP-Method</a>; Journal of the American Chemical Society; Vol. 79; No. 3; 609-615; <a href="https://doi.org/10.1021/ja01560a028">10.1021/ja01560a028</a></li>
<li>Schroeder, W. A. and LeGette, Joann (1953) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181120-153101208">A Study of the Quantitative Dinitrophenylation of Amino Acids and Peptides</a>; Journal of the American Chemical Society; Vol. 75; No. 18; 4612-4615; <a href="https://doi.org/10.1021/ja01114a531">10.1021/ja01114a531</a></li>
<li>Schroeder, W. A. and Honnen, Lewis R. (1953) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181120-153101121">Correlation between the Structure of Some Dinitrophenyl Peptides and their Chromatographic Behavior on Silicic Acid—Celite</a>; Journal of the American Chemical Society; Vol. 75; No. 18; 4615-4619; <a href="https://doi.org/10.1021/ja01114a532">10.1021/ja01114a532</a></li>
<li>Schroeder, W. A. and Honnen, Lewis, el al. (1953) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SCHRpnas53">Chromatographic separation and identification of some peptides in partial hydroylsates of gelatin</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 39; No. 1; 23-30</li>
<li>Schroeder, W. A. (1952) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181120-153101033">Sequence of four amino acids at the end of the single polypeptide chain of lysozyme</a>; Journal of the American Chemical Society; Vol. 74; No. 1; 281-282; <a href="https://doi.org/10.1021/ja01121a528">10.1021/ja01121a528</a></li>
<li>Schroeder, W. A. and Kay, Lois M., el al. (1950) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SCHRjbc50">Amino acid composition of hemoglobins of normal Negroes and sickle-cell anemics</a>; Journal of Biological Chemistry; Vol. 187; No. 1; 221-240</li>
<li>Zechmeister, L. and LeRosen, A. L., el al. (1943) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180727-101437995">Spectral Characteristics and Configuration of Some Stereoisomeric Carotenoids Including Prolycopene and Pro-γ-carotene</a>; Journal of the American Chemical Society; Vol. 65; No. 10; 1940-1951; <a href="https://doi.org/10.1021/ja01250a039">10.1021/ja01250a039</a></li>
<li>Zechmeister, L. and Schroeder, W. A. (1942) <a href="https://resolver.caltech.edu/CaltechAUTHORS:ZECjbc42a">The fruit of Pyracantha angustifolia: a practical source of pro-γ-carotene and prolycopene</a>; Journal of Biological Chemistry; Vol. 144; No. 2; 315-320</li>
</ul>