Peptides comprising the bulk of rat brain extracts: isolation, amino acid sequences and biological activity

Autor: Olga A. Kalinina, Igor V. Nazimov, Elena Yu. Blishchenko, Marina M. Philippova, Oleg N. Yatskin, Vadim T. Ivanov, Andrei A. Karelin
Rok vydání: 2000
Předmět:
Zdroj: Journal of Peptide Science. 6:345-354
ISSN: 1099-1387
1075-2617
DOI: 10.1002/1099-1387(200008)6:8<345::aid-psc258>3.0.co;2-u
Popis: Chromatographic separation of rat brain extracts followed by automatic Edman sequencing of the major individual components resulted in identification of 61 endogenous peptides derived from known functional proteins (hemoglobin, myelin basic protein, cytochrome-c oxidase, etc.) or unknown precursors. The results are compared with the data obtained earlier for bovine brain. Although the sequences of bovine and rat hemoglobin contain about 20% of amino acid substitutions, the families of structurally related peptides are very similar in both extracts. Several other proteins also give rise to identical or closely related peptide fragments in the two mammalian species. The outlined similarity extends almost exclusively to the most abundant peptides present in the extracts. The minor components show less overlap. Four hemoglobin-derived peptides isolated from rat brain were shown to be biologically active in tumor cells. Eleven are identical to bioactive peptides from other species. Ten structurally overlap with bioactive peptides from other sources. The data obtained show similar biosynthetic pathways of pool components in different species, the resultant peptides being aimed at fulfilling related functions. Copyright © 2000 European Peptide Society and John Wiley & Sons, Ltd.
Databáze: OpenAIRE
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