The Separation and Amino Acid Composition of the Tryptic Peptides of the a Chain of Hemoglobin from C57BL Mice*

نویسنده

  • RAYMOND A. POPP
چکیده

Hemoglobin is a conjugated protein composed of heme prosthetic groups united to polypeptide chains. The structure, four heme groups associated with four polypeptide chains, seems to be similar for all mammalian hemoglobins (1). Usually the polypeptide chains appear in two forms, which in adults are called a and @ chains. Homology occurs among the polypeptide chains of hemoglobins partially because of the common evolution of mammals. The extent to which homology is maintained because of a relationship between the structure and function of hemoglobin is not known. Presumably, amino acid substitutions can occur in positions that are not, or are at least less, essential for hemoglobin’s specific function of oxygen transport. Analyses of the amino acid sequences in the polypeptide chains of hemoglobins from many different species of mammals, as well as within species, should aid in the determination of the sites in the polypeptide chains that interact with the heme group to assist its oxygen transport mechanisms. Multiple forms of hemoglobin occur among highly inbred strains of laboratory mice (%4), and there appears to be much similarity between the ac and @ chains of human and mouse hemoglobins. This report describes the separation of the tryptic peptides and the determination of the amino acid composition of the OL chain of hemoglobin from strain C57BL mice. The results are compared with those of human hemoglobin. Similar studies on the /3 chain are being done elsewhere.’

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The Separation and Amino Acid Composition of the Tryptic Peptides of the Alpha Chain of Hemoglobin from C57bl Mice.

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تاریخ انتشار 2003