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短密青霉鸟嘌呤特异性核糖核酸酶的氨基酸序列和二硫键

Amino acid sequence and S-S bonds of Penicillium brevicompactum guanyl-specific ribonuclease.

作者信息

Shlyapnikov S V, Kulikov V A, Yakovlev G I

出版信息

FEBS Lett. 1984 Nov 19;177(2):246-8. doi: 10.1016/0014-5793(84)81292-2.

DOI:10.1016/0014-5793(84)81292-2
PMID:6437869
Abstract

The primary structure of Penicillium brevicompactum guanyl-specific RNase was determined. The enzyme consists of 102 amino acid residues, Mr 10801. The 4 cysteine residues of the RNase are linked in pairs by disulfide bonds: Cys2-Cys10, Cys6-Cys101. P. brevicompactum RNase structure is similar to RNase T1; the degree of homology is 66%.

摘要

确定了短密青霉鸟嘌呤特异性核糖核酸酶的一级结构。该酶由102个氨基酸残基组成,分子量为10801。核糖核酸酶的4个半胱氨酸残基通过二硫键成对连接:Cys2-Cys10,Cys6-Cys101。短密青霉核糖核酸酶的结构与核糖核酸酶T1相似;同源程度为66%。

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Amino acid sequence and S-S bonds of Penicillium brevicompactum guanyl-specific ribonuclease.短密青霉鸟嘌呤特异性核糖核酸酶的氨基酸序列和二硫键
FEBS Lett. 1984 Nov 19;177(2):246-8. doi: 10.1016/0014-5793(84)81292-2.
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引用本文的文献

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Microbial ribonucleases (RNases): production and application potential.微生物核糖核酸酶(RNases):生产及应用潜力
World J Microbiol Biotechnol. 2015 Dec;31(12):1853-62. doi: 10.1007/s11274-015-1945-8. Epub 2015 Oct 3.
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Tertiary structure of RNase Pch1 predicted from the model structure of RNase Ms and the crystal structure of RNase T1. Comparison among the model structures--testing the limits of modelling by homology.
Eur Biophys J. 1990;18(4):225-33. doi: 10.1007/BF00183375.