通过ADP核糖基化实现核糖核酸酶的可逆失活。

Reversible inactivation of ribonucleases by ADPribosylation.

作者信息

Leone E, Farina B, Faraone Mennella M R

出版信息

Biochim Biophys Acta. 1986 Jun 5;871(2):182-8. doi: 10.1016/0167-4838(86)90172-x.

Abstract

The activity of purified bovine seminal RNAase and pancreatic RNAase A (EC 3.1.27.5) has been investigated following in vitro ADPribosylation in the presence of nuclear ADPribosyltransferase (EC 2.4.2.30) and NAD+ X ADPribosylation of these enzymes was correlated with a significant decrease in their activities. Approximately three residues of ADPribose were present per mol of enzyme. Removal of the bound ADPribose restored enzyme activity to near normal levels. Similar results were obtained with nuclei isolated from bull seminal vesicles as an endogenous source of seminal RNAase and nuclear ADPribosyltransferase. The findings suggest that in vitro ADPribosylation has a reversible inactivating effect on ribonucleases.

摘要

在存在核ADP核糖基转移酶（EC 2.4.2.30）和NAD⁺的情况下进行体外ADP核糖基化后，对纯化的牛精浆核糖核酸酶和胰腺核糖核酸酶A（EC 3.1.27.5）的活性进行了研究。这些酶的ADP核糖基化与它们活性的显著降低相关。每摩尔酶中大约存在三个ADP核糖残基。去除结合的ADP核糖可使酶活性恢复到接近正常水平。以从公牛精囊中分离的细胞核作为精浆核糖核酸酶和核ADP核糖基转移酶的内源性来源，也获得了类似的结果。这些发现表明，体外ADP核糖基化对核糖核酸酶具有可逆的失活作用。