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Primary structure and biological activity of hemoglobin‐related hypothalamic peptides
Author(s) -
Galoyan A. A.
Publication year - 1997
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1997)43:2<135::aid-bip6>3.0.co;2-w
Subject(s) - chemistry , hemoglobin , calmodulin , protein primary structure , biochemistry , peptide , amino acid , peptide sequence , primary (astronomy) , hemoglobin variants , biological activity , amino acid residue , enzyme , in vitro , gene , physics , astronomy
Five individual fractions from bovine hypothalamic extract, displaying coronary constrictory activity, were isolated and sequenced. All of them belong to the hemorphin group of hemoglobin‐derived peptides. These peptides bind calmodulin and activate calmodulin‐dependent enzymes. The relationship of isolated peptides with other members of the hemorphin group is discussed. Several new fragments of hemoglobin α‐ and β‐chains with yet unidentified activity were obtained from the same source. Their amino acid sequences have considerable overlap with the known sequences of hemoglobin fragments isolated from other tissues. © 1997 John Wiley & Sons, Inc. Biopoly 43: 135–137, 1997