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黄色短杆菌中谷氨酸脱氢酶的分离纯化及特性
引用本文:陆卫平,张剑,王浩,郑善良.黄色短杆菌中谷氨酸脱氢酶的分离纯化及特性[J].复旦学报(自然科学版),1988(4).
作者姓名:陆卫平  张剑  王浩  郑善良
作者单位:复旦大学微生物学与微生物工程系,复旦大学微生物学与微生物工程系,复旦大学微生物学与微生物工程系,复旦大学微生物学与微生物工程系 1985届本科毕业生,1985届本科毕业生
摘    要:经硫酸铵盐析、DEAE-纤维素层析、苯-琼脂糖CL-4B(Phenyl-SepharoseOL-4B)层析和交联葡聚糖G-200(Sephadex G-200)层析等步骤从谷氨酸产生菌——黄色短杆菌中分离纯化的谷氨酸脱氢酶,酶活提高了230倍。该酶的分子量约为30万,由六个分子量约为5万的亚基组成,最适pH为8.9,并对热较稳定。在pH8.2时,以谷氨酸和NADP+为底物时的米氏常数值分别为0.294mol/L和0.1mmol/L。

关 键 词:谷氨酸脱氢酶  黄色短杆菌  提纯。

PURIFICATION AND CHARACTERIZATION OF GLUTAMATE DEHYDROGENASE FROM Brevibacterium flavum
Lu Weiping,Zhang Jian,Wang Hao,Zheng Shanliang,.PURIFICATION AND CHARACTERIZATION OF GLUTAMATE DEHYDROGENASE FROM Brevibacterium flavum[J].Journal of Fudan University(Natural Science),1988(4).
Authors:Lu Weiping  Zhang Jian  Wang Hao  Zheng Shanliang  
Institution:Department of Microbiology and Microbial Technology
Abstract:Glutamate dehydrogenase was purified 230-fold from Brevibacterium flavum byammonium sulphate fractionation, and chromatographies on DEAE-cellulose,Phenyl-Sepharose CL-4B and Sephadex G-200. The enzyme had a molecular weightof about 300 000, consisting of six subunits each with a molecular weight of 50 000. Itexhibited a single band after electrophoresis on SDS-polyacrylamide gel, a K_m of0.294 mol/L and 0.1mmol/L for glutamate and NADP~+, respectively. It had a pHoptimum around 8.9 and showed a medium thermo-stability.
Keywords:glutamate dehydrogenase  brevibacterium flavum  purification  
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