Proteolytic degradation of hemoglobin in erythrocytes leads to biologically active peptides

A number of hemoglobin-derived homogenous 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 we...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1995, Vol.16 (4), p.693-697
Main Authors: Karelin, Andrey A., Philippova, Marina M., Ivanov, Vadim T.
Format: Article
Language:English
Subjects:
Adult
Amino Acid Sequence
Erythrocytes - metabolism
Female
Hemoglobin
Hemoglobins - metabolism
HPLC
Human
Humans
Hydrolysis
Isolation
Male
Molecular Sequence Data
Neo-kyotorphin
Peptide fragments
Peptide Fragments - blood
Precursor
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Summary:A number of hemoglobin-derived homogenous 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.
ISSN:0196-9781
1873-5169
DOI:10.1016/0196-9781(95)00029-J