首页> 外文期刊>Journal of bacteriology >Conservation of primary structure of the pyridoxyl peptide of Escherichia coli and Serratia marcescens tryptophan synthase beta2 protein.
【24h】

Conservation of primary structure of the pyridoxyl peptide of Escherichia coli and Serratia marcescens tryptophan synthase beta2 protein.

机译:大肠埃希氏杆菌和粘质沙雷氏菌色氨酸合酶β2蛋白的一级结构的保守性。

获取原文
           

摘要

Two labeled peptides were recovered from tryptic digests of the NaB3H4-reduced, performic acid-oxidized beta2 protein of Serratia marcescens tryptophan synthase. These two pyridoxyl peptides were identical except for the presence or absence of an NH2-terminal arginyl residue. Tryptic digestion of nonreduced, performic acid-oxidized protein allowed isolation of the peptides that comprise the two halves of the pyridoxyl peptide. The partial primary structure for this region of the protein was shown to be Arg-Glx-Asx-Ler-Leu-His(Gly,Gly,Ala,His)Lys(Pxy)-Thr-Asx-Glx-Val(Leu,Gly,Glx,Ala,Leu,Leu,Ala)Lys. All the data available indicate that the sequence is identical with the homologous region from the Escherichia coli enzyme.
机译:从NaB3H4还原的,粘质沙雷氏菌色氨酸合酶的过甲酸氧化的β2蛋白的胰蛋白酶消化物中回收了两个标记的肽。除了存在或不存在NH 2-末端精氨酰基残基外,这两个吡啶氧基肽是相同的。对未还原的,过甲酸氧化的蛋白质进行胰蛋白酶消化,可以分离出包含吡啶氧酰肽两半的肽。该蛋白区域的部分一级结构显示为Arg-Glx-Asx-Ler-Leu-His(Gly,Gly,Ala,His)Lys(Pxy)-Thr-Asx-Glx-Val(Leu,Gly ,Glx,Ala,Leu,Leu,Ala)所有可用的数据表明该序列与大肠杆菌酶的同源区域相同。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号