Proteolytic degradation of hemoglobin in erythrocytes leads to biologically active peptides.
A number of hemoglobin-derived homogeneous peptides were isolated from erythrocyte lysate. The amino acid sequences of nine peptides were determined. Seven out of nine peptides were relatively long, 30-32 membered peptides covering the N- or C-terminal sequences of globin chains. The remaining two were the pentapeptide neo-kyotorphin and its tetrapeptide derivative.
D000328:Adult; D000595:Amino Acid Sequence; D004912:Erythrocytes / Q000378:metabolism*; D005260:Female; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000097:blood*
D006454:Hemoglobins; D010446:Peptide Fragments