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鼠伤寒沙门氏菌LT2硫酸结合蛋白的氨基酸序列。

Amino acid sequence of the sulfate-binding protein from Salmonella typhimurium LT2.

作者信息

Isihara H, Hogg R W

出版信息

J Biol Chem. 1980 May 25;255(10):4614-8.

PMID:6989815
Abstract

The amino acid sequence of the sulfate-binding protein from Salmonella typhimurium LT2 was determined by automated sequenator analysis of whole protein and fragments derived by chemical and enzymatic cleavage of whole protein. The fragments were products of limited trypsin digestion at arginine, cleavage at tryptophan by BrNps-skatole and o-iodosobenzoic acid, digestion with the protease from Staphylococcus aureus V8 at Glu-X bonds, cleavage by hydroxylamine at Asn-Gly bonds, and subdigestion with trypsin, chymotrypsin, and the Staphylococcus protease. The COOH-terminal sequence was confirmed using carboxypeptidase B and amino acid analysis. The sulfate-binding protein was determined to contain a single polypeptide of 310 residues with a molecular weight of 34,667 calculated from the sequence.

摘要

通过对完整蛋白质以及通过化学和酶促切割完整蛋白质得到的片段进行自动测序仪分析,确定了鼠伤寒沙门氏菌LT2硫酸结合蛋白的氨基酸序列。这些片段是在精氨酸处进行有限胰蛋白酶消化、用溴化氰-粪臭素和邻碘苯甲酸在色氨酸处切割、用金黄色葡萄球菌V8蛋白酶在Glu-X键处消化、用羟胺在Asn-Gly键处切割以及用胰蛋白酶、胰凝乳蛋白酶和葡萄球菌蛋白酶进行亚消化的产物。使用羧肽酶B和氨基酸分析确认了COOH末端序列。经测定,硫酸结合蛋白含有一条由310个残基组成的单一多肽链,根据序列计算其分子量为34,667。

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