Primary structure and biological activity of hemoglobin-related hypothalamic peptides
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Updated: Aug 15, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
1Institute of Biochemistry, NAS RA, Yerevan, Republic of Armenia.
Insights
Researchers isolated novel hemorphin peptides from bovine hypothalamus that constrict coronary arteries by activating calmodulin-dependent enzymes. These findings reveal new hemoglobin-derived peptides with potential cardiovascular implications.
Area of Science:
- Biochemistry
- Cardiovascular Science
- Neuroendocrinology
Background:
- Hemoglobin-derived peptides, known as hemorphins, have diverse biological activities.
- The bovine hypothalamus is a source of bioactive peptides.
- Calmodulin-dependent enzymes play crucial roles in cellular signaling.
Purpose of the Study:
- To isolate and characterize novel peptides from bovine hypothalamic extract with coronary constrictory activity.
- To determine the relationship of these peptides to the known hemorphin group.
- To investigate the mechanism of action involving calmodulin.
Main Methods:
- Peptide isolation and sequencing from bovine hypothalamic extract.
- Assay of coronary constrictory activity.
- Calmodulin binding assays and activation of calmodulin-dependent enzymes.
Main Results:
- Five individual fractions with coronary constrictory activity were isolated and sequenced.
- All identified fractions belong to the hemorphin group of hemoglobin-derived peptides.
- These hemorphins bind calmodulin and activate calmodulin-dependent enzymes.
- New hemoglobin alpha- and beta-chain fragments with unknown activity were also identified.
Conclusions:
- Novel hemorphins from the bovine hypothalamus exhibit coronary constrictory effects.
- The mechanism involves calmodulin binding and activation of downstream enzymes.
- These findings expand the known repertoire of hemorphins and their physiological roles.
- Further research is warranted to explore the therapeutic potential of these peptides.
Abstract:
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.
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