通过与2,3 - 二甲基马来酸酐可逆缩合实现牛6S前羧肽酶A的解离：应用于亚基III的部分表征
Dissociation of bovine 6S procarboxypeptidase A by reversible condensation with 2,3-dimethyl maleic anhydride: application to the partial characterization of subunit III.
作者信息
Puigserver A, Desnuelle P
出版信息
Proc Natl Acad Sci U S A. 1975 Jun;72(6):2442-5. doi: 10.1073/pnas.72.6.2442.
Abstract
Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish. Therefore, this subunit is likely to be a chymotrypsinogen or proelastase-A-like zymogen which has lost the ability to be activated on account of a deletion of the N-terminal residues from half-cystine 1 to valine 17. Like other pancreatic zymogens, subunit III appears to possess a weakly functional active site.
摘要
牛6S前羧肽酶A可通过用顺丁烯二酸酐酰化而解离成其三个亚基。由于在接近中性的pH值下与顺丁烯二酸二甲酯的键不稳定，脱酰化的亚基以基本上天然的形式获得。亚基III的前七个残基与牛胰凝乳蛋白酶原B的残基18 - 24相同，并且与牛胰凝乳蛋白酶原A和C（亚基II）以及非洲肺鱼的前弹性蛋白酶A中的相同残基非常相似。因此，该亚基可能是一种胰凝乳蛋白酶原或前弹性蛋白酶A样的酶原，由于从半胱氨酸1到缬氨酸17的N端残基缺失而失去了被激活的能力。与其他胰腺酶原一样，亚基III似乎具有弱功能的活性位点。
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