赤子爱胜蚓中一种聚-L-赖氨酸激活的丝氨酸内切蛋白酶的纯化与特性分析
Purification and characterization of a poly-L-lysine-activated serine endoprotease from Lumbricus rubellus.
作者信息
Woo K M, Yi W, Sohn Y J, Chang C S, Kang M S, Ha D B, Chung C H
机构信息
Department of Molecular Biology, College of Natural Sciences, Seoul National University, Korea.
出版信息
Comp Biochem Physiol B Biochem Mol Biol. 1994 Sep;109(1):71-80. doi: 10.1016/0305-0491(94)90143-0.
PMID:7842229
Abstract
An endoprotease in earthworm (Lumbricus rubellus) is purified to apparent homogeneity using 125I-lactalbumin as a substrate. The protease has a molecular mass of 27 kDa and is markedly activated by poly-L-lysine or poly-L-arginine. It is a chymotrypsin-like serine protease. Its activity is distributed to coelomic fluid but relatively little to coelomocytes.
摘要
以125I-乳白蛋白为底物，将赤子爱胜蚓中的一种内蛋白酶纯化至表观均一。该蛋白酶的分子量为27 kDa，被聚-L-赖氨酸或聚-L-精氨酸显著激活。它是一种类胰凝乳蛋白酶丝氨酸蛋白酶。其活性分布于体腔液中，但在体腔细胞中的分布相对较少。
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