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[溶菌酶制剂溶菌酰胺酶。溶菌肽酶L1的纯化及某些性质]

[Bacteriolytic enzyme preparation lysoamidase. Purification and some properties of bacteriolytic peptidase L1].

作者信息

Stepanaia O A, Begunova E A, Tsfasman I M, Kulaev I S

出版信息

Biokhimiia. 1996 Apr;61(4):656-63.

PMID:8724784
Abstract

The bacteriolytic peptidase L1 has been isolated from the enzyme preparation of lysoamidase capable to lyze cell walls of gram-positive bacteria using ion-exchange chromatography and gel filtration. Some physico-chemical properties of the enzyme have been established. The molecular mass of L1 is 21 kDa, the pH optimum for Staphylococcus aureus cell lysis is 7-11. The optimal concentration of the buffer is 50 mM; the temperature optimum is 70 degrees C; the half-inactivation temperature is 55 degrees C.

摘要

已使用离子交换色谱法和凝胶过滤法从能够裂解革兰氏阳性菌细胞壁的溶菌酰胺酶的酶制剂中分离出溶菌肽酶L1。已确定了该酶的一些物理化学性质。L1的分子量为21 kDa,裂解金黄色葡萄球菌细胞的最适pH为7-11。缓冲液的最佳浓度为50 mM;最适温度为70℃;半失活温度为55℃。

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