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[某些酶在KMT羧基阳离子交换剂上的离子交换纯化]

[Ion exchange purification of some enzymes on KMT carboxyl cation exchanges].

作者信息

Pappel K E, Kaljula H J, Sakalauskaite N J, Letunova E V, Tikhomirova A S, Shatayeva L K, Samsonov G V

出版信息

Prikl Biokhim Mikrobiol. 1975 Jul-Aug;11(4):598-600.

PMID:813204
Abstract

Highly purfied preparations of the enzymes--yeast beta-fructofuranosidase, fungal beta-galactosidase and bacterial proteases have been isolated from crude preparations or culture liquids by adsorption on KMT microporous carboxyl cation exchanger. During desorption the enzyme activity has fully recovered and the specific activity increased 4.5-fold for beta-galactosidase and 54-fold for proteases.

摘要

已通过吸附在KMT微孔羧基阳离子交换剂上,从粗制品或培养液中分离出了高度纯化的酶制剂——酵母β-呋喃果糖苷酶、真菌β-半乳糖苷酶和细菌蛋白酶。在解吸过程中,酶活性完全恢复,β-半乳糖苷酶的比活性提高了4.5倍,蛋白酶的比活性提高了54倍。

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