Amino acid sequence of human D of the alternative complement pathway.
Amino acid sequence of human D of the alternative complement pathway.
复制标题
补体旁路途径人 D 的氨基酸序列。
DOI：
10.1021/bi00306a025
复制
发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Volanakis,JE
中科院分区：
文献类型：
--
作者：
Niemann,MA;Bhown,AS;Bennett,JC;Volanakis,JE
玛丽莲·A Niemann，* Ajit S. Bhown，J. Claude班尼特和John E. Volanakis摘要：人D是一种丝氨酸蛋白酶，激活替代性补体途径的C3转化酶，它的一级结构是通过对各种化学（CNBr和邻碘苯甲酸）和酶（胰蛋白酶、赖氨酸蛋白酶、金黄色葡萄球菌V8蛋白酶和胰凝乳蛋白酶）裂解产生的肽段进行测序而推导出来的。羧肽酶A也用于确认COOH-末端序列。通过高压液相色谱法纯化肽。推测的人D基因序列由222个氨基酸组成，分子量为23748。它与其他丝氨酸蛋白酶具有高度的同源性，尤其是在NH 2-末端周围以及对应于活性位点His-57、Asp-102和Ser-195（胰凝乳蛋白酶原编号）的三个残基。该序列与纤溶酶的同源性最高（40%），居中（35%）
Marilyn A. Niemann,* Ajit S. Bhown, J. Claude Bennett, and John E. Volanakis abstract: The primary structure of human D, the serine protease activating the C3convertase of the alternative com-plement pathway, has been deducedby sequencing peptides derived from various chemical (CNBr and o-iodosobenzoic acid) and enzymatic (trypsin, lysine protease, Staphylococcus aureus V8 protease, and chymotrypsin) cleavages. Carboxypeptidase A was also used to confirm the COOH-terminal sequence. The peptides were purified by high-pressure liquid chromatography. The proposed sequence of human D contains 222 amino acids andhas a calculated molecular weight of 23 748. It exhibits a high degree of homology with otherserine proteases, especially around the NH2-terminus as well as the three residues corresponding to the active-site His-57, Asp-102, and Ser-195 (chymotrypsinogen numbering). This sequence homology is highest (40%) with plasmin, intermediate (35%)