Purification and characterization of a calcium dependent sulfhydryl protease from human platelets.
Purification and characterization of a calcium dependent sulfhydryl protease from human platelets.
复制标题
从人血小板中纯化和表征钙依赖性巯基蛋白酶。
DOI：
10.1016/s0006-291x(81)80247-1
复制
发表时间：
1981
影响因子：
3.1
通讯作者：
Stracher,A
中科院分区：
文献类型：
--
作者：
Truglia,JA;Stracher,A
一种钙依赖性巯基蛋白酶（CDSP）负责超过95%的人血小板中性蛋白酶活性已被纯化。CDSP由分子量估计为80，000和30，000道尔顿的两种不同的多肽亚基组成。它需要毫摩尔钙，减少巯基和中性pH值的最佳活性。它被亮抑酶肽和在纯化过程中去除的内源性抑制剂抑制。CDSP特异性地将血小板的肌动蛋白结合蛋白（F-肌动蛋白微丝的交联剂）切割成两个高分子量片段，其中较重的片段仍保留其结合F-肌动蛋白的能力，但不交联成细胞骨架阵列。
A calcium dependent sulfhydryl protease (CDSP) responsible for over 95% of the neutral protease activity of human platelets has been purified. CDSP is composed of two different polypeptide subunits of molecular weights estimated to be 80,000 and 30,000 daltons. It requires millimolar calcium, reduced sulfhydryl groups and neutral pH for optimal activity. It is inhibited by Leupeptin and an endogenous inhibitor which is removed during purification. CDSP specifically cleaves the platelet's Actin Binding Protein, crosslinker of F-actin microfilaments, into two high molecular weight fragments, the heavier of which still retains its ability to bind to, but not crosslink F-actin into cytoskeletal arrays.