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鸟嘌呤特异性核糖核酸酶和鸟嘌呤优先核糖核酸酶的亚位点结构。寡聚肌苷酸和多聚I的切割

The subsite structures of guanine-specific ribonucleases and a guanine-preferential ribonuclease. Cleavage of oligoinosinic acids and poly I.

作者信息

Watanabe H, Ando E, Ohgi K, Irie M

出版信息

J Biochem. 1985 Nov;98(5):1239-45. doi: 10.1093/oxfordjournals.jbchem.a135390.

Abstract

In order to estimate the size of the active site of guanylic acid specific RNases (RNase T1 from Aspergillus oryzae and RNase St from Streptomyces erythreus) and guanine-preferential RNase (RNase Ms from A. saitoi), the depolymerization reaction of oligoinosinic acid, (Ip)nI greater than p, having various chain lengths was studied. The kinetic parameters for depolymerization of oligoinosinic acids, (pKm, log V and log V/Km) by the three RNases increased with increase of the chain length of the substrates, and became almost constant at n = 2 or more. Thus, the size of the active site of RNase T1, RNase St, and RNase Ms was estimated to be three nucleotides in length.

摘要

为了估算鸟苷酸特异性核糖核酸酶(米曲霉核糖核酸酶T1和红霉素链霉菌核糖核酸酶St)以及鸟嘌呤优先核糖核酸酶(斋藤曲霉核糖核酸酶Ms)活性位点的大小,研究了具有不同链长的寡聚肌苷酸((Ip)nI>p)的解聚反应。三种核糖核酸酶对寡聚肌苷酸解聚的动力学参数(pKm、logV和logV/Km)随着底物链长的增加而增加,在n = 2或更大时几乎保持恒定。因此,核糖核酸酶T1、核糖核酸酶St和核糖核酸酶Ms的活性位点大小估计为三个核苷酸长度。

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