猪胰弹性蛋白酶相关酸性内肽酶和胰凝乳蛋白酶C的鉴定。
The identity of the elastase-associated acidic endopeptidase and chymotrypsin C from porcine pancreas.
作者信息
Thomson A, Denniss I S
出版信息
Biochim Biophys Acta. 1976 Apr 8;429(2):581-90. doi: 10.1016/0005-2744(76)90306-5.
The preparations of chymotrypsin C (EC 3.4.21.2) and an acidic endopeptidase from porcine pancreas have been repeated using published procedures. The acidic endopeptidase showed lower activity than chymotrypsin C in all comparative experiments, but it was possible to precipitate a fraction from the acidic endopeptidase preparation which contained all the protein and was identical with chymotrypsin C. It is concluded that the acidic endopeptidase is identical with chymotrypsin C but it is contaminated by an inert non-protein material to which it is firmly bound. The formation of a precipitate, at low ionic strength, from mixtures of chymotrypsin C and elastase (EC 3.4.21.11) is independent of the availability of the active site of either enzyme.
已按照已发表的方法重复制备了胰凝乳蛋白酶C（EC 3.4.21.2）和来自猪胰腺的一种酸性内肽酶。在所有对比实验中，该酸性内肽酶的活性均低于胰凝乳蛋白酶C，但有可能从酸性内肽酶制剂中沉淀出一部分，其包含了所有蛋白质且与胰凝乳蛋白酶C相同。得出的结论是，该酸性内肽酶与胰凝乳蛋白酶C相同，但被一种与之紧密结合的惰性非蛋白质物质所污染。在低离子强度下，胰凝乳蛋白酶C和弹性蛋白酶（EC 3.4.21.11）混合物形成沉淀与这两种酶中任一种酶活性位点的可用性无关。
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