Primary structure and biological activity of hemoglobin-related hypothalamic peptides.
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 alpha- and beta-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.
Galoyan
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AA
Institute of Biochemistry, NAS RA, Yerevan, Republic of Armenia.
D000595:Amino Acid Sequence; D000818:Animals; D002147:Calmodulin / Q000378:metabolism; D002403:Cathepsins / Q000378:metabolism; D006454:Hemoglobins / Q000737:chemistry*; D007031:Hypothalamus / Q000737:chemistry*; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D010974:Platelet Aggregation / Q000187:drug effects; D017421:Sequence Analysis; D014662:Vasoconstrictor Agents / Q000737:chemistry / Q000494:pharmacology
D002147:Calmodulin; D006454:Hemoglobins; D010446:Peptide Fragments; D014662:Vasoconstrictor Agents; D002403:Cathepsins