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从大肠杆菌中分离腺苷酸环化酶。

Isolation of adenyl cyclase from Escherichia coli.

作者信息

Tao M, Lipmann F

出版信息

Proc Natl Acad Sci U S A. 1969 May;63(1):86-92. doi: 10.1073/pnas.63.1.86.

Abstract

We have found a soluble cyclase, using for assay radioactively marked ATP as precursor. The reaction product was isolated by thin-layer chromatography and identified by specific degradation. After homogenization, part of the activity remained in the particulate fraction but could be easily extracted. The cyclase was concentrated 100-fold by conventional methods. The enzyme has a Mg(++) requirement and is inhibited by fluoride and inorganic pyrophosphate.

摘要

我们发现了一种可溶性环化酶,使用放射性标记的ATP作为前体进行测定。反应产物通过薄层色谱法分离,并通过特异性降解进行鉴定。匀浆后,部分活性保留在颗粒部分,但很容易提取出来。通过常规方法将环化酶浓缩了100倍。该酶需要Mg(++),并受到氟化物和无机焦磷酸的抑制。

相似文献

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Isolation of adenyl cyclase from Escherichia coli.从大肠杆菌中分离腺苷酸环化酶。
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