Abood L G, Hong J S, Takeda F, Tometsko A M
Biochim Biophys Acta. 1976 Sep 7;443(3):414-27. doi: 10.1016/0005-2736(76)90461-2.
A number of hydrophobic proteins have been separated and purified to varying degrees from synaptic membranes derived from bovine brain. The proteins, which have been obtained using preparative acrylamide gel electrophoresis, have been analyzed for molecular weight, amino acid composition, peptide mapping, N-terminal amino acids, and for their ability to bind calcium and ATP. A number of the proteins bound calcium, the greatest binding being associated with a component having a molecular weight of 1.6 - 10(4), a binding capacity of 4 calcium/molecule, and a Km of 1.5 - 10(-5) M. An acidic tryptic peptide derived from this protein was evidently responsible for the calcium-binding. ATP binding appeared to be confined largely to the higher molecular weight proteins. From the peptide mapping there appears to be a similar acidic component in a number of the proteins exhibiting calcium-binding. ATP-binding was associated mainly with the high molecular weight proteins, particularly those which consisted of numerous basic tryptic peptides.
已从牛脑来源的突触膜中分离并不同程度地纯化出多种疏水蛋白。这些蛋白是通过制备性丙烯酰胺凝胶电泳获得的，已对其分子量、氨基酸组成、肽图谱、N 端氨基酸以及结合钙和 ATP 的能力进行了分析。许多蛋白能结合钙，最强的结合作用与一种分子量为 1.6×10⁴ 的成分相关，其结合能力为每分子结合 4 个钙，米氏常数为 1.5×10⁻⁵ M。源自该蛋白的一种酸性胰蛋白酶肽显然负责钙结合。ATP 结合似乎主要局限于较高分子量的蛋白。从肽图谱来看，许多具有钙结合能力的蛋白中似乎存在类似的酸性成分。ATP 结合主要与高分子量蛋白相关，尤其是那些由众多碱性胰蛋白酶肽组成的蛋白。
