Zuckerkandl, Emile and Jones, Richard T. and Pauling, Linus (1960) A comparison of animal hemoglobins by tryptic peptide pattern analysis. Proceedings of the National Academy of Sciences of the United States of America, 46 (10). pp. 1349-1360. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:ZUCpnas60
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The complete amino acid sequences (primary structure) of hemoglobins can, in principle, be determined by methods currently available. Although detailed studies of the primary structure of human and horse hemoglobins are in progress in several laboratories,(1) the methods are so laborious that complete sequences have not yet been established. Important questions in the realm of genetics and evolution require the immediate examination of the structure, primary and other, of many different hemoglobins. The application of methods that are quicker, though less informative and reliable, than the techniques required for complete sequence determination is therefore in order as a provisional means of securing useful information. Such a method is the analysis of peptide patterns obtained by combined paper electrophoresis and chromatography of tryptic hydrolysates of denatured hemoglobin.(2) Of particular interest are comparisons between hemoglobin components present in (a) organisms of one animal species at a given time in development, (b) organisms of one species at different stages of development, and (c) organisms of different species. The present paper is concerned exclusively with the last type of comparison. In order to scan the range of variation of hemoglobin structure throughout evolution, hemoglobins from a number of animals both closely and distantly related to man have been selected and compared as to tryptic peptide patterns with human hemoglobin A. Whole hemoglobin preparations from adult animals have been studied throughout. The problem of individual heterogeneity will be treated elsewhere.
|Additional Information:||Copyright © 1960 by the National Academy of Sciences. Communicated August 22, 1960. This work was supported in part by Grant No. H3136 from the National Institutes of Health, U.S. Public Health Service, and was presented in part at the 138th meeting of the American Chemical Society. Division of Chemistry and Chemical Engineering, California Institute of Technology, Contribution No. 2618.|
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|Deposited By:||Tony Diaz|
|Deposited On:||18 Jan 2006|
|Last Modified:||26 Dec 2012 08:44|
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