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从大鼠肝细胞培养物中纯化具有促增殖活性的多肽及其一级结构。与人类胰岛素样生长因子II的同源性。

Purification and primary structure of a polypeptide with multiplication-stimulating activity from rat liver cell cultures. Homology with human insulin-like growth factor II.

作者信息

Marquardt H, Todaro G J, Henderson L E, Oroszlan S

出版信息

J Biol Chem. 1981 Jul 10;256(13):6859-65.

PMID:7016879
Abstract

A low molecular weight polypeptide with multiplication-stimulating activity (MSA) was isolated from serum-free media conditioned by a clone of normal Buffalo rat liver cells. The purification of MSA was achieved by gel permeation chromatography of the acid-soluble growth-promoting activity on Bio-Gel P-10 in 1 M acetic acid and followed by reversed phase high pressure liquid chromatography on muBondapak C18 support using a linear gradient of acetonitrile in 0.05% trifluoroacetic acid. The primary structure of MSA has been determined. MSA is a single chain polypeptide of 67 residues, with a calculated molecular weight of 7,484, and displays 93% homology with the functionally related human insulin-like growth factor II (IGF-II). A comparison between the sequences of rat MSA and human IGF-II reveals only five amino acid substitutions. Based on the extensive amino acid sequence homology, we propose the term rat IGF-II for this newly isolated polypeptide.

摘要

从正常布法罗大鼠肝细胞克隆的无血清培养基中分离出一种具有增殖刺激活性（MSA）的低分子量多肽。通过在1M乙酸中对Bio-Gel P-10上的酸溶性生长促进活性进行凝胶渗透色谱法，然后在μBondapak C18载体上使用乙腈在0.05%三氟乙酸中的线性梯度进行反相高压液相色谱法，实现了MSA的纯化。已确定MSA的一级结构。MSA是一种由67个残基组成的单链多肽，计算分子量为7484，与功能相关的人胰岛素样生长因子II（IGF-II）具有93%的同源性。大鼠MSA和人IGF-II序列之间的比较仅发现五个氨基酸替换。基于广泛的氨基酸序列同源性，我们将这种新分离的多肽命名为大鼠IGF-II。

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