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pubmed-article:9643629pubmed:abstractTextFractionation of bovine brain extracts followed by automatic Edman sequencing of individual components resulted in identification of 107 endogenous peptides formed from functional proteins (haemoglobin, myelin basic protein, cytochrome c oxidase, etc) or unknown precursors. Several of the newly identified brain peptides demonstrate different types of biological activity; some of the substances show considerable overlap with the known biologically active peptides. It is suggested that these peptides should participate in regulation of extracellular and intracellular biochemical processes. A concept of 'tissue-specific peptide pool' is formulated describing a novel system of peptidergic regulation, complementary to the conventional hormonal and neuromodulatory systems. According to that description functional proteins provide their proteolytically derived fragments for maintaining the tissue homeostasis by modulating the availability of peptide receptors to respective 'true' ligands.lld:pubmed
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pubmed-article:9643629pubmed:authorpubmed-author:KarelinA AAAlld:pubmed
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pubmed-article:9643629pubmed:pagination211-25lld:pubmed
pubmed-article:9643629pubmed:dateRevised2003-11-14lld:pubmed
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pubmed-article:9643629pubmed:year1998lld:pubmed
pubmed-article:9643629pubmed:articleTitlePeptides from bovine brain: structure and biological role.lld:pubmed
pubmed-article:9643629pubmed:affiliationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.lld:pubmed
pubmed-article:9643629pubmed:publicationTypeJournal Articlelld:pubmed