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由质粒pIE 636编码的乙酰转移酶使诺尔斯菌素(链丝菌素)失活:失活产物中N-乙酰-β-赖氨酸的检测

[Nourseothricin (streptothricin) inactivated by plasmid pIE 636-encoded acetyltransferase: detection of N-acetyl-beta-lysine in the inactivated product].

作者信息

Seltmann G

出版信息

Zentralbl Bakteriol Mikrobiol Hyg A. 1985 Dec;260(4):421-2. doi: 10.1016/s0176-6724(85)80061-4.

Abstract

Nourseothricin (streptothricin) can be inactivated by an acetyl transferase synthesized by E. coli strains containing plasmid pIE 636. Nourseothricin inactivated in the presence of 14C-acetyl-coenzyme A was purified and submitted to partial acidic hydrolysis. By electrophoresis of the hydrolysate a 14C-containing substance moving only slowly towards the cathode could be isolated. This substance after complete hydrolysis yields only unlabelled beta-lysine.

摘要

诺尔斯菌素(链丝菌素)可被含有质粒pIE 636的大肠杆菌菌株合成的乙酰转移酶灭活。在14C-乙酰辅酶A存在下被灭活的诺尔斯菌素经纯化后进行部分酸性水解。通过对水解产物进行电泳,可分离出一种仅缓慢向阴极移动的含14C的物质。该物质完全水解后仅产生未标记的β-赖氨酸。

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Localization of a streptothricin acetyl transferase in cells of Escherichia coli K-12.
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