[The place of carnosine among physiologically active peptides].
| Autor: | Zamiatnin AA |
|---|---|
| Jazyk: | ruština |
| Zdroj: | Biokhimiia (Moscow, Russia) [Biokhimiia] 1992 Sep; Vol. 57 (9), pp. 1296-301. |
| Abstrakt: | The results of analysis of EROP-Moscow data base concerning structural and functional peculiarities of endogenous regulatory oligopeptides are reviewed in relation to carnosine, the first endogenous peptide bioregulator. The dipeptide fragment ala-his is widely distributed in natural systems, in particular in various representatives of living organisms. The main structural peculiarity of carnosine is its elongated "filamentous" structure with a positively charged N-terminus and a cyclic radical characteristic of large physiologically active oligopeptides. The relatedness of carnosine to other oligopeptides also becomes apparent during the analysis of its role in various regulatory systems of the body. |
| Databáze: | MEDLINE |
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