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人转化生长因子β2的完整氨基酸序列。

Complete amino acid sequence of human transforming growth factor type beta 2.

作者信息

Marquardt H, Lioubin M N, Ikeda T

出版信息

J Biol Chem. 1987 Sep 5;262(25):12127-31.

PMID:3476488
Abstract

The complete amino acid sequence of human type beta 2 transforming growth factor (hTGF-beta 2) was determined by automated Edman degradation of S-pyridylethylated hTGF-beta 2 and selected fragments. Cleavage of hTGF-beta 2 by enzymatic and chemical techniques established all the fragments in an unambiguous sequence. Human TGF-beta 2 consists of two disulfide-linked, identical subunits. Each hTGF-beta 2 subunit is a single-chain polypeptide of 112 residues, with a calculated molecular weight of 12,720. Human TGF-beta 2 displays 71.4% sequence homology with the functionally related human TGF-beta 1, and is distantly related (23-40% amino acid identity) to porcine inhibins and activins, the carboxyl-terminal regions of human Müllerian inhibiting substance, and the putative decapentaplegic gene complex protein of Drosophila.

摘要

通过对S-吡啶基乙基化的人β2型转化生长因子(hTGF-β2)及其选定片段进行自动Edman降解,确定了人β2型转化生长因子(hTGF-β2)的完整氨基酸序列。通过酶促和化学技术对hTGF-β2进行切割,确定了所有片段的明确序列。人转化生长因子-β2由两个通过二硫键连接的相同亚基组成。每个hTGF-β2亚基是一个由112个残基组成的单链多肽,计算分子量为12,720。人转化生长因子-β2与功能相关的人转化生长因子-β1显示出71.4%的序列同源性,并且与猪抑制素和激活素、人苗勒管抑制物质的羧基末端区域以及果蝇假定的decapentaplegic基因复合体蛋白有较远的关系(氨基酸同一性为23-40%)。

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