Researches on the influence of 3-hydroxy-3-methylglutary-coenzyme A reductase gene polymorphism on catalytic efficiency of its encode enzyme in Glycyrrhiza uralensis.
- Author:
Ying LIU
1
;
Qiao-Xian XU
;
Xue-Yong WANG
;
Chun-Sheng LIU
;
Hong-Hao CHEN
Author Information
- Publication Type:Journal Article
- MeSH: Biocatalysis; Chromatography, Thin Layer; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Escherichia coli; genetics; Gas Chromatography-Mass Spectrometry; Glycyrrhiza uralensis; enzymology; genetics; Hydroxymethylglutaryl CoA Reductases; genetics; metabolism; Mutation; Plant Proteins; genetics; metabolism; Polymorphism, Genetic; Recombinant Proteins; metabolism
- From: China Journal of Chinese Materia Medica 2012;37(24):3784-3788
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo analyse the effect of expression proteins containing different escherichia coli of 3-hydroxy-3-methylglutary-coenzyme A reductase(HMGR) genic mutation on the conversion efficiency of MVA with GC-MS method, in order to lay a foundation for revealing the function of HMGR gene polymorphism of Glycyrrhiza uralensis in the production of high-quality G. uralensis medicines.
METHODThe expression carrier was established from four HMGR genic mutation types cloned from G. uralensis and transformed into Escherichia coli BL21. The protein was induced to express, detected and purified. The purified protein was adopted for in vitro enzymatic reaction. TLC and GC-MS were used for qualitative and quantitative analysis on reaction products.
RESULTThe catalytic activity of L/V genotype(-HSL and -HSV) was similar, and so was the catalytic activity of the genotype with GA insertion (GALLV and GALSV), but the catalytic activity of the latter was around 2 times higher than that of the former.
CONCLUSIONThe functional gene polymorphism of G. uralensis may be the molecular foundation for the production of high-quality G. uralensi medicines.
