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Two L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity.

作者信息

Campbell H A, Mashburn L T, Boyse E A, Old L J

出版信息

Biochemistry. 1967 Mar;6(3):721-30. doi: 10.1021/bi00855a011.

DOI:10.1021/bi00855a011
PMID:5337885
Abstract
摘要

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Two L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity.来自大肠杆菌B的两种L-天冬酰胺酶。它们的分离、纯化及抗肿瘤活性。
Biochemistry. 1967 Mar;6(3):721-30. doi: 10.1021/bi00855a011.
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Localization of the two-L-asparaginases in anaerobically grown Escherichia coli.
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Glutaminase activity of L-asparagine amidohydrolase.L-天冬酰胺酰胺水解酶的谷氨酰胺酶活性
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Regulation of glutaminase B in Escherichia coli. I. Purification, properties, and cold lability.大肠杆菌中谷氨酰胺酶B的调控。I. 纯化、性质及冷不稳定特性
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Two L-asparaginases from E. coli and their action against tumors.来自大肠杆菌的两种L-天冬酰胺酶及其抗肿瘤作用。
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Partial purification and antilymphoma activity of Serratia marcescens L-asparaginase.粘质沙雷氏菌L-天冬酰胺酶的部分纯化及抗淋巴瘤活性
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[Bacterial L-asparaginase and glutamin(asparagin)ase: some properties, structure and anti-tumor activity].[细菌L-天冬酰胺酶和谷氨酰胺(天冬酰胺)酶:一些特性、结构和抗肿瘤活性]
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L-asparagine amidohhdrolase (E. C. 3.5.1.1.) in a commercial preparation of Escherichia coli ATCC 11246. Some properties of the enzyme and its possible use in the determination of l-asparagine.大肠杆菌ATCC 11246商业制剂中的L-天冬酰胺酰胺水解酶(E.C. 3.5.1.1.)。该酶的一些性质及其在L-天冬酰胺测定中的可能用途。
Acta Chem Scand. 1967;21(9):2573-5. doi: 10.3891/acta.chem.scand.21-2573.
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TUMOR INHIBITORY EFFECT OF L-ASPARAGINASE FROM ESCHERICHIA COLI.大肠杆菌L-天冬酰胺酶的肿瘤抑制作用
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L-glutamine as a substrate for L-asparaginase from Serratia marcescens.L-谷氨酰胺作为粘质沙雷氏菌L-天冬酰胺酶的底物。
J Bacteriol. 1974 Feb;117(2):593-600. doi: 10.1128/jb.117.2.593-600.1974.

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