[从荧光假单胞菌AG中纯化脱酰胺酶AG（天冬酰胺酶-谷氨酰胺酶）及其一些物理化学性质]
[Purification of deamidase AG (asparaginase-glutaminase) from Pseudomonas fluorescens AG and some physicochemical properties of the enzyme].
作者信息
Mardashev S R, Nikolaev A Ia, Kovalenko N A, Rakov S S, Tsvetkova T A
出版信息
Vopr Med Khim. 1975 Jan-Feb;21(1):29-35.
PMID:804211
Abstract
Deamidase AG (asparaginase-glutaminase) was obtained from Pseudomonas fluorescens in a crystalline apparently homogenous state. Molecular weight of the enzyme, determined by acrylamide gel electrophoresis, was equal to 128 000 daltons; by ultracentrifugation (56100 rev/min, 65 min, 20.5 degrees C) coefficient of sedimentation was shown to be 7.36 S. Optimal pH for asparaginase activity of the enzyme was at pH 8.0-9.0, for glutaminase activity--at pH 5.5-7.5.
摘要
脱酰胺酶AG（天冬酰胺酶 - 谷氨酰胺酶）以晶体状且明显均一的状态从荧光假单胞菌中获得。通过丙烯酰胺凝胶电泳测定，该酶的分子量为128000道尔顿；通过超速离心法（56100转/分钟，65分钟，20.5摄氏度）测定，沉降系数为7.36 S。该酶天冬酰胺酶活性的最适pH为8.0 - 9.0，谷氨酰胺酶活性的最适pH为5.5 - 7.5。
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