[Biospecific preparation and some properties of molecular factors, interacting with brain-specific proteins S100].
The biospecific preparation and a preliminary analysis of physico-chemical properties of water-soluble proteins from bovine brain and liver and brain oligopeptides specifically adsorbed on a column with immobilized brain-specific proteins of the major fraction S100 were carried out. Using thin-layer electrophoresis on cellulose and tachyphoresis, it was found that four oligopeptide cations and three anionic oligopeptides interact with S100. Polyacrylamide gel electrophoresis revealed at least six brain proteins and 11 liver proteins, which interact with S100. An essential role in interaction of protein ligands from the bran (but not from liver) with immobilized S100 proteins belongs to Ca2+. The use of natural endogenous ligands for the study of the biological role of brain-specific proteins S100 is discussed.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D008024:Ligands; D008099:Liver / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*; D009842:Oligopeptides / Q000032:analysis; D009928:Organ Specificity; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism; D009418:S100 Proteins / Q000302:isolation & purification* / Q000378:metabolism
D008024:Ligands; D009419:Nerve Tissue Proteins; D009842:Oligopeptides; D011506:Proteins; D009418:S100 Proteins; D002118:Calcium
Biospetsificheskoe vydelenie i nekotorye svoĭstva molekuliarnykh faktorov, vzaimodeĭstvuiushchikh s mozgospetsificheskimi belkami gruppy S100.