辣根过氧化物酶同工酶C。大肠杆菌转化体产生的天然酶和重组酶的比较研究。

Horseradish peroxidase isozyme C. A comparative study of native and recombinant enzyme produced by E. coli transformants.

作者信息

Egorov A M, Gazaryan I G, Kim B B, Doseyeva V V, Kapeljuch J L, Veryovkin A N, Fechina V A

机构信息

Chemistry Department, Lomonosov Moscow University, Russia.

出版信息

Ann N Y Acad Sci. 1994 May 2;721:73-81. doi: 10.1111/j.1749-6632.1994.tb47378.x.

DOI:10.1111/j.1749-6632.1994.tb47378.x

PMID:8010699

Abstract

The purification and refolding of the recombinant horseradish peroxidase produce by E. coli transformants are described. The recombinant enzyme is of 34 kDa and has an isozyme spectrum similar to Sigma type VI horseradish peroxidase. The specific activity of the refolded peroxidase is of about 2000 U/mg with ABTS as a substrate. The recombinant and native enzyme are similar with respect to their catalytic properties in the reaction of enhanced chemiluminescence. Operational and thermal stability of the refolded peroxidase is two to three times lower than for the native one.

摘要

描述了由大肠杆菌转化体产生的重组辣根过氧化物酶的纯化和重折叠。该重组酶分子量为34 kDa，具有与Sigma VI型辣根过氧化物酶相似的同工酶谱。以ABTS为底物时，重折叠过氧化物酶的比活性约为2000 U/mg。在增强化学发光反应中，重组酶和天然酶的催化特性相似。重折叠过氧化物酶的操作稳定性和热稳定性比天然酶低两到三倍。