Abstract：Glutamine Synthetase(GS) from Gorynebacterium pekinense AS 1.299 was partially purified by heat denaturation,ammonium sulfate precipitation and DEAE-cellulose chromatography.Further purification was carried out with polyacrylami-ide slab gel electrophoresis.The Km values of GS for hydroxylamine and L-gluta-mine were 43.5 rnM and 16.4 mM respectively.The sedimentation coefficient of GS was 21S.MW of subunit of the enzyme obtained by SDS electrophoresis was 56,000 dalton.Chemical modification of GS indicated that sulfhydryl group,try-ptophan and arginine residues had no relation to enzyme activity.Modifying reagents of tyrosine caused remarkable decrease in the enzyme activity.And histidyl-residues were essential groups for enzyme activity.
钱世钧,郝凤兮,孟广震,姜维真,刘晓灿. 北京棒状杆菌AS1.299谷氨酰胺合成酶的提纯和性质[J]. 中国生物化学与分子生物学报, 1986, 2(02): 37-42.
Qian,Shi-jun Hao,Feng-xi Meng,Guang-zhenJiang,Wei-zhen Liu,Xiao-can. PURIFICATION AND PROPERTIES OF GLUTAMINE S Y NTHETASE FROM CORYNEBACTERIUM PEKINENSE AS 1.299. Chinese Journal of Biochemistry and Molecular Biol, 1986, 2(02): 37-42.
