嗜盐嗜碱杆菌丝氨酸蛋白酶的纯化及性质
Purification and properties of serine protease from Halobacterium halobium.
作者信息
Izotova L S, Strongin A Y, Chekulaeva L N, Sterkin V E, Ostoslavskaya V I, Lyublinskaya L A, Timokhina E A, Stepanov V M
出版信息
J Bacteriol. 1983 Aug;155(2):826-30. doi: 10.1128/jb.155.2.826-830.1983.
Abstract
Pure extracellular serine protease was isolated from the culture filtrate of Halobacterium halobium by bacitracin-Sepharose affinity chromatography. The enzyme activity was completely and irreversibly lost if the NaCl concentration fell below 2 M. The protease consists of one polypeptide chain with a molecular weight of 41,000. It is characteristically enriched in Asx and Glx content, whereas the level of basic amino acids in the enzyme molecule is unusually low. The protease shows a preference for leucine in the carboxylic side of the scissile bond of the substrate, cleaving the B-chain of oxidized bovine insulin only at the Leu15-Tyr16 bond and liberating p-nitroaniline from L-pyroglutamyl-L-alanyl-L-alanyl-L-leucine-p-nitroanilide.
摘要
通过杆菌肽-琼脂糖亲和色谱法从嗜盐嗜盐菌的培养滤液中分离出纯细胞外丝氨酸蛋白酶。如果氯化钠浓度降至2M以下，酶活性将完全不可逆地丧失。该蛋白酶由一条分子量为41,000的多肽链组成。其特征是天冬氨酸和谷氨酸含量丰富，而酶分子中碱性氨基酸的水平异常低。该蛋白酶在底物可裂解键的羧基侧对亮氨酸有偏好，仅在Leu15-Tyr16键处切割氧化牛胰岛素的B链，并从L-焦谷氨酰-L-丙氨酰-L-丙氨酰-L-亮氨酸-对硝基苯胺中释放对硝基苯胺。
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