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反式-N-脱氧核糖基酶:通过亲和层析法纯化及特性鉴定

Trans-N-deoxyribosylase: purification by affinity chromatography and characterization.

作者信息

Holguin J, Cardinaud R

出版信息

Eur J Biochem. 1975 Jun;54(2):505-14. doi: 10.1111/j.1432-1033.1975.tb04163.x.

Abstract

trans-N-Deoxyribosylase (EC 2.4.2.6) is usually considered as a single protein catalyzing indifferently the transfer of the deoxyribosyl moiety to and from a purine or a pyrimidine base. Affinity chromatography of an extract from Lactobacillus helveticus with two types of ligands allowed the separation and purification of two distinct trans-N-deoxyribosylases. One catalyzes specifically the deoxyribosyl transfer to and from purine bases exclusively: trans-N-deoxyribosylase-I, the other catalyzes the transfer to and from pyrimidine and purine bases: trans-N-deoxyribosylase-II. A Tris inhibition study showed a markedly different susceptibility of the two enzymes. Preliminary results indicate that the purine-specific enzyme is a polymeric enzyme of molecular weight 86 000 (+/- 4000).

摘要

反式-N-脱氧核糖基酶(EC 2.4.2.6)通常被认为是一种单一蛋白质,它无差别地催化脱氧核糖基部分与嘌呤或嘧啶碱基之间的转移。用两种类型的配体对瑞士乳杆菌提取物进行亲和层析,可分离和纯化出两种不同的反式-N-脱氧核糖基酶。一种专门催化脱氧核糖基仅在嘌呤碱基之间的转移:反式-N-脱氧核糖基酶-I,另一种催化脱氧核糖基在嘧啶和嘌呤碱基之间的转移:反式-N-脱氧核糖基酶-II。Tris抑制研究表明这两种酶的敏感性明显不同。初步结果表明,嘌呤特异性酶是一种分子量为86000(±4000)的聚合酶。

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