GLUCOSE-6-PHOSPHATE DEHYDROGENASE FROM ESCHERICHIA-COLI AND FROM A HIGH-LEVEL MUTANT

GLUCOSE-6-PHOSPHATE DEHYDROGENASE FROM ESCHERICHIA-COLI AND FROM A HIGH-LEVEL MUTANT
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DOI:
10.1128/jb.110.1.155-160.1972
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发表时间:
1972-01-01
影响因子:
3.2
通讯作者:
FRAENKEL, DG
FRAENKEL, DG
中科院分区:
生物学3区
文献类型:
--
作者:
BANERJEE, S;FRAENKEL, DG

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6-磷酸葡萄糖脱氢酶已从野生型大肠杆菌 K-12 和先前发现含有大量该酶的突变体中纯化至接近同质。迄今为止研究的这两种酶的所有特征都是相同的:比活性、动力学、特异性和亚基大小。
Glucose-6-phosphate dehydrogenase has been purified to near homogeneity from wild-typeEscherichia coliK-12 and from a mutant previously found to contain substantially more of the enzyme. The two enzymes are the same in all characteristics studied thus far: specific activity, kinetics, specificity, and subunit size.