ACTIVATION OF BOVINE FACTOR-VII (PROCONVERTIN) BY FACTOR-XIIA (ACTIVATED HAGEMAN-FACTOR)
ACTIVATION OF BOVINE FACTOR-VII (PROCONVERTIN) BY FACTOR-XIIA (ACTIVATED HAGEMAN-FACTOR)
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DOI：
10.1021/bi00638a009
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发表时间：
1977-01-01
期刊：
影响因子：
2.9
通讯作者：
DAVIE, EW
中科院分区：
文献类型：
--
作者：
KISIEL, W;FUJIKAWA, K;DAVIE, EW
牛凝血因子VII（前转化素）是一种血浆糖蛋白，参与血液凝固的外源性途径。其分子量为45，500，由一条具有氨基末端丙氨酸残基的单链多肽链组成。采用1：50的酶与底物重量比，因子VII容易被因子XIIa（活化的Hageman因子）转化为因子VIIa。因子VIIa由通过二硫键结合在一起的L和H链组成。由前体羧基末端区域形成的H链含有Ile-Val-Gly-Gly-的氨基末端序列。H链还含有-Phe-Cys-Ala-Gly-Tyr-Thr-Asp-Gly-Thr-Lys-Asp-Ala-Cys-Lys-Gly-Asp-Ser-Gly-Gly-Pro-His-的活性位点序列。该序列与许多血浆丝氨酸蛋白酶的活性位点区域同源。因子VII是丝氨酸蛋白酶的典型前体，其被因子XIIa通过切割单个内部肽键转化为酶。
Bovine factor VII (proconvertin) is a plasma glycoprotein that participates in the extrinsic pathway of blood coagulation. It has a MW of 45,500 and is composed of a single polypeptide chain with an amino-terminal alanine residue. Factor VII is readily converted to factor VIIa by factor XIIa (activated Hageman factor) employing an enzyme to substrate weight ratio of 1:50. Factor VIIa is composed of a L and H chain held together by a disulfide bond(s). The H chain, which is formed from the carboxyl-terminal region of the precursor, contains an aminoterminal sequence of Ile-Val-Gly-Gly-. The H chain also contains the active-site sequence of -Phe-Cys-Ala-Gly-Tyr-Thr-Asp-Gly-Thr-Lys-Asp-Ala-Cys-Lys-Gly-Asp-Ser-Gly-Gly-Pro-His-. This sequence is homologous with the active-site region of a number of plasma serine proteases. Factor VII is a typical precursor of a serine protease which is converted to an enzyme by factor XIIa by the cleavage of a single, internal peptide bond.