IMMUNOAFFINITY PURIFICATION OF TRANSKETOLASES FROM YEAST AND SPINACH LEAVES

被引：5

作者：

DEMUYNCK, C ^{[1
]}

FISSON, F ^{[1
]}

BENNANIBAITI, I ^{[1
]}

SAMAKI, H ^{[1
]}

MANI, JC ^{[1
]}

机构：

[1] UNIV CLERMONT FERRAND,CHIM ORGAN BIOL LAB,CNRS,UA 485,CLERMONT FERRAND,FRANCE

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1990年 / 54卷 / 12期

关键词：

D O I：

10.1080/00021369.1990.10870464

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

Transketolase (TK, EC 2.2.1.1) was purified from bakers' yeast and spinach leaves by immunoaffinity using rabbit polyclonal anti-TK antibodies, which had been purified by immunoaffinity on immobilized TK, and coupled to Trisacryl. This enzyme is a useful tool for the synthesis of chiral ketoses. The properties of the enzymes from both origins were compared.

引用

页码：3073 / 3078

页数：6

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