ACTIVATION OF BOVINE FACTOR-X (STUART FACTOR) - CONVERSION OF FACTOR XA-ALPHA TO FACTOR XA-BETA
ACTIVATION OF BOVINE FACTOR-X (STUART FACTOR) - CONVERSION OF FACTOR XA-ALPHA TO FACTOR XA-BETA
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DOI：
10.1073/pnas.72.9.3359
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发表时间：
1975-01-01
影响因子：
11.1
通讯作者：
DAVIE, EW
中科院分区：
文献类型：
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作者：
FUJIKAWA, K;TITANI, K;DAVIE, EW
牛凝血因子X(分子量55,100)是一种凝血因子，以前体或酶原形式存在于血浆中。它是一种糖蛋白，通过一个或多个二硫键以两链结构形式被分离出来。在凝血过程中，凝血因子X通过重链氨基末端的特定多肽键的水解转化为丝氨酸蛋白酶。这种切割发生在Arg-51和Ile-52之间，产生Xapha因子(分子量45,300)和活化肽(分子量9500)。然后，通过在重链的羧基末端区域的第二个特定的多肽键的水解，将XaAlpha因子转化为Xabeta因子(分子量为42,600)。这种切割发生在Arg-290和Gly-291之间，产生第二个糖肽(分子量2700)。Xapha因子和Xabeta因子具有相同的凝血活性，表明第二个肽键的断裂与激活过程无关。
Bovine factor X (molecular weight 55,100) is a blood coagulation factor present in plasma in a precursor or zymogen form. It is a glycoprotein which has been isolated as a two-chain structure held together by one or more disulfide bonds. During the coagulation process, factor X is converted to a serine protease by the hydrolysis of a specific peptide bond in the amino-terminal region of the heavy chain. This cleavage occurs between Arg-51 and Ile-52, giving rise to factor Xaalpha (molecular weight 45,300) and an activation peptide (molecular weight 9500). Factor Xaalpha is then converted to factor Xabeta (molecular weight 42,600) by hydrolysis of a second specific peptide bond in the carboxyl-terminal region of the heavy chain. This cleavage occurs between Arg-290 and Gly-291, giving rise to a second glycopeptide (molecular weight 2700). Factor Xaalpha and factor Xabeta have equivalent coagulant activity, indicating that the cleavage of the second peptide bond is unrelated to the activation process.