大肠杆菌055:B5来源的L-天冬酰胺酶EC-2的纯化及性质
Purification and properties of L-asparaginase EC-2 from Escherichia coli 055:B5.
作者信息
Pajdak E, Szafran Z
出版信息
Acta Biochim Pol. 1977;24(1):53-8.
PMID:17256
Abstract
- L-Asparaginase has been isolated from aerobically grown Escherichia coli 055:B5 and purified about 140-fold in a three-step procedure involving acidification to pH 4.5, ammonium sulphate fractionation and column chromatography on DEAE-Sephadex A-50. The activity of the preparation is 140 U/mg protein. 2. The enzyme acts within a broad pH range (pH 5-9) and is affected neither by PCMB, N-ethylmaleimide nor metal ions. 3. Molecular weight of the isolated asparaginase is 130 000.
摘要
- L-天冬酰胺酶已从需氧培养的大肠杆菌055:B5中分离出来，并通过三步程序纯化了约140倍，该程序包括酸化至pH 4.5、硫酸铵分级分离和在DEAE-葡聚糖A-50上进行柱色谱。该制剂的活性为140 U/mg蛋白质。2. 该酶在较宽的pH范围（pH 5-9）内起作用，不受对氯汞苯甲酸、N-乙基马来酰亚胺和金属离子的影响。3. 分离出的天冬酰胺酶的分子量为130 000。
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