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大肠杆菌中代谢中间体与β-半乳糖苷酶之间的相互作用。

Interactions between metabolic intermediates and beta-galactosidase from Escherichia coli.

作者信息

Moses V, Sharp P B

出版信息

Biochem J. 1970 Jul;118(3):491-5. doi: 10.1042/bj1180491.

Abstract
  1. 5-Phosphorylribose 1-pyrophosphate, in the presence of beta-mercaptoethanol, protected beta-galactosidase from heat inactivation. Many other substances, including 3':5'-cyclic-AMP, were without effect. 2. The efficiency of complementation in vitro of beta-galactosidase segments was decreased by 5-phosphorylribose 1-pyrophosphate but not by 3':5'-cyclic-AMP. Neither substance affected the activity of the complete enzyme. 3. Some indications as to the possible identity of the catabolite repression effector are presented.
摘要
  1. 在β-巯基乙醇存在的情况下,5-磷酸核糖1-焦磷酸可保护β-半乳糖苷酶免受热失活。包括3':5'-环磷酸腺苷在内的许多其他物质则无此作用。2. 5-磷酸核糖1-焦磷酸可降低β-半乳糖苷酶片段体外互补的效率,但3':5'-环磷酸腺苷不会。这两种物质均不影响完整酶的活性。3. 文中给出了一些关于分解代谢物阻遏效应物可能身份的线索。

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Adenosine 3':5'-cyclic monophosphate and catabolite repression in Escherichia coli.
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The isolation and properties of beta-galactosidase from Escherichia coli grown on sodium selenate.
Biochim Biophys Acta. 1967 Aug 29;141(3):587-99. doi: 10.1016/0304-4165(67)90187-0.

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