Tryptic Peptide Compositions of Hemoglobins from Mink (Hustela Vison) and Hyena (Hyaenae Hyaenae) and the α-Chain of coatmundi (Nasua Nasua

B. Brimhall Department of Biochemistry School of Medicine, University of Oregon Health Sciences Center Portland, Oregon, 97201; Department of Biochemistry and Biophysics, Oregon State University Corvallis, Oregon, 97331

Kenneth Stangland Department of Biochemistry School of Medicine, University of Oregon Health Sciences Center Portland, Oregon, 97201; Department of Biochemistry and Biophysics, Oregon State University Corvallis, Oregon, 97331

R. T. Jones Department of Biochemistry School of Medicine, University of Oregon Health Sciences Center Portland, Oregon, 97201; Department of Biochemistry and Biophysics, Oregon State University Corvallis, Oregon, 97331

Robert R. Becker Department of Biochemistry School of Medicine, University of Oregon Health Sciences Center Portland, Oregon, 97201; Department of Biochemistry and Biophysics, Oregon State University Corvallis, Oregon, 97331

Thomas J. Bailey Department of Biochemistry School of Medicine, University of Oregon Health Sciences Center Portland, Oregon, 97201; Department of Biochemistry and Biophysics, Oregon State University Corvallis, Oregon, 97331

Abstract

The amino acid composition of the tryptic peptides from hyena hemoglobin, two hemoglobins of the mink and the α-chain of coatimundi have been deterimined, allowing comparison with data previously obtained from other carnivores. The two hemoglobins of mink differ at only one amino acid residue, α15, which is glycyl in one hemoglobin and as party 1 in the other.

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Tryptic Peptide Compositions of Hemoglobins from Mink (Hustela Vison) and Hyena (Hyaenae Hyaenae) and the α-Chain of coatmundi (Nasua Nasua

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Tryptic Peptide Compositions of Hemoglobins from Mink (Hustela Vison) and Hyena (Hyaenae Hyaenae) and the α-Chain of coatmundi (Nasua Nasua

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