Davidson L, Brear D R, Wingard P, Hawkins J, Kitto G B
J Bacteriol. 1977 Mar;129(3):1379-86. doi: 10.1128/jb.129.3.1379-1386.1977.
An enzyme that catalyzes the hydrolysis of both glutamine and asparagine has been purified to homogeneity from extracts of Pseudomonas acidovorans. The enzyme having a ratio of glutaminase to asparaginase of 1.45:1.0 can be purified by a relatively simple procedure and is stable upon storage. The glutaminase-asparaginase has a relatively high affinity for L-asparagine (Km=1.5 X 10(-5) M) and L-glutamine (Km=2.2 X 10(-5) M) and has a molecular weight of approximately 156,000 the subunit molecular weight being approximately 39,000. Injections of the enzyme produced only slight increases in the survival time of C3H/HE mice carrying the asparagine-requiring 6C2HED Gardner lymphoma and of white Swiss mice carrying the glutamine-requiring Ehrlich lymphoma.
一种能催化谷氨酰胺和天冬酰胺水解的酶已从食酸假单胞菌提取物中纯化至同质。这种谷氨酰胺酶与天冬酰胺酶比例为1.45:1.0的酶可通过相对简单的程序纯化，且储存时稳定。谷氨酰胺酶 - 天冬酰胺酶对L - 天冬酰胺（Km = 1.5×10⁻⁵ M）和L - 谷氨酰胺（Km = 2.2×10⁻⁵ M）具有相对较高的亲和力，分子量约为156,000，亚基分子量约为39,000。注射该酶后，携带需要天冬酰胺的6C2HED加德纳淋巴瘤的C3H/HE小鼠以及携带需要谷氨酰胺的艾氏淋巴瘤的瑞士小白鼠的存活时间仅略有增加。
