N-terminal degradation of ACTH(4-10) and its synthetic analog semax by the rat blood enzymes
| Autor: | V. N. Nezavibat'ko, N.G. Levitzkaya, V.N. Potaman, A.A. Kamensky, L.Y. Alfeeva |
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| Rok vydání: | 1991 |
| Předmět: |
Male
Kinetics Biophysics Semax Reaction intermediate Peptide hormone Biochemistry Aminopeptidase High-performance liquid chromatography Adrenocorticotropic Hormone In vivo Leucine medicine Animals Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification Chemistry Hydrolysis Rats Inbred Strains Cell Biology Peptide Fragments Rats Enzyme medicine.drug |
| Zdroj: | Biochemical and biophysical research communications. 176(2) |
| ISSN: | 0006-291X |
| Popis: | Summary Degradation of a regulatory peptide ACTH(4–10) and its synthetic analog semax in rat blood and serum was studied using high-performance liquid chromatography. About one third to one half of the serum degrading activity could be ascribed to bestatin-sensitive aminopeptidase which cleaved first and second N-terminal residues Met and Glu producing relatively stable intermediates. Comparable areas under the degradation/accumulation curves for intact peptides and intermediates implied that the latter can contribute to effects of intact peptides. Semax turned out to be more stable than ACTH(4–10) against the action of other enzymes that took part in degradation. |
| Databáze: | OpenAIRE |
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