[与脑特异性蛋白S100相互作用的分子因子的生物特异性制备及其某些特性]
[Biospecific preparation and some properties of molecular factors, interacting with brain-specific proteins S100].
作者信息
Poletaev A B, Beliaev S V, Lysova N P
出版信息
Biokhimiia. 1982 Aug;47(8):1349-53.
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.
进行了牛脑和肝脏水溶性蛋白质以及特异性吸附在固定有主要组分S100脑特异性蛋白质的柱上的脑寡肽的生物特异性制备及其物理化学性质的初步分析。通过纤维素薄层电泳和快速电泳发现，有四种寡肽阳离子和三种阴离子寡肽与S100相互作用。聚丙烯酰胺凝胶电泳显示，至少有六种脑蛋白和十一种肝蛋白与S100相互作用。脑（而非肝脏）的蛋白质配体与固定化S100蛋白相互作用中，Ca2+起着重要作用。讨论了使用天然内源性配体研究脑特异性蛋白质S100的生物学作用。
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