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牛心线粒体ADP/ATP载体的完整氨基酸序列

Complete amino acid sequence of the ADP/ATP carrier from beef heart mitochondria.

作者信息

Aquila H, Misra D, Eulitz M, Klingenberg M

出版信息

Hoppe Seylers Z Physiol Chem. 1982 Mar;363(3):345-9.

PMID:7076130
Abstract

The complete primary structure of the ADP/ATP carrier from beef heart mitochondria is described. Cyanogen bromide cleaves the protein into a long, N-terminally blocked fragment with Mr 22,000 (CB1) and several small peptides. The primary information was derived from liquid-phase sequencing of tryptic peptides obtained from the maleylated carrier protein and the citraconylated CB1 fragment, as well as from cleavage products with Staphylococcus aureus protease. The multitude of thermolysinolytic, tryptic, chymotryptic and peptic peptides was sequenced by manual methods. They rendered overlaps and further supported already known partial sequences. Also, the bridge between the published acidolytic C-terminal fragment A2 was thus obtained.

摘要

本文描述了牛心线粒体ADP/ATP载体的完整一级结构。溴化氰将该蛋白质切割成一个Mr为22,000的长的、N端封闭的片段(CB1)和几个小肽段。主要信息来自对从马来酰化载体蛋白和柠康酰化CB1片段获得的胰蛋白酶肽段的液相测序,以及来自金黄色葡萄球菌蛋白酶切割产物的测序。通过手工方法对大量嗜热菌蛋白酶、胰蛋白酶、胰凝乳蛋白酶和胃蛋白酶肽段进行了测序。它们形成了重叠,并进一步支持了已知的部分序列。此外,由此获得了已发表的酸解C端片段A2之间的连接。

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