风疹蚓聚赖氨酸活化丝氨酸内蛋白酶的纯化及特性研究

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-09-01 DOI:10.1016/0305-0491(94)90143-0

Kee Min Woo , Woelsung Yi , Young Jong Sohn , Chung-Soon Chang , Man-Sik Kang , Doo Bong Ha , Chin Ha Chung

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引用次数: 7

摘要

以125i -乳清蛋白为底物纯化了一种具有明显同质性的内蛋白酶。该蛋白酶分子量为27kda，可被聚赖氨酸或聚精氨酸显著激活。它是一种类似凝乳胰蛋白酶的丝氨酸蛋白酶。其活性分布于体腔液中，但相对较少分布于体腔细胞中。

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Purification and characterization of a poly-l-lysine-activated serine endoprotease from Lumbricus rubellus

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.

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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry

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