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从牛骨中纯化和鉴定一种独特的骨诱导因子。

Purification and characterization of a unique osteoinductive factor from bovine bone.

作者信息

Bentz H, Nathan R M, Rosen D M, Armstrong R M, Thompson A Y, Segarini P R, Mathews M C, Dasch J R, Piez K A, Seyedin S M

机构信息

Celtrix Laboratories, Collagen Corporation, Palo Alto, California 94303.

出版信息

J Biol Chem. 1989 Dec 5;264(34):20805-10.

PMID:2584240
Abstract

A unique protein that promotes ectopic osteoinduction in the rat has been isolated and characterized. Osteoinductive factor (OIF) was extracted from the organic matrix of bovine bone with 4 M guanidine HCl and purified by gel filtration, ion-exchange chromatography, affinity chromatography, and reversed phase high performance liquid chromatography. OIF is a glycoprotein with an apparent molecular mass of 22-28 kDa based on sodium dodecyl sulfate gel electrophoresis. Enzymatic or chemical deglycosylation of OIF reduces its mass to about 12 kDa with apparent loss of activity. OIF activity in the model used is substantially increased by addition of transforming growth factor (TGF)-beta 1 or TGF-beta 2, suggesting an important role for TGF-beta 1 and -2 in bone regeneration and repair. The N-terminal sequence of OIF has no homology to other reported proteins.

摘要

一种能促进大鼠异位骨诱导的独特蛋白质已被分离和鉴定。骨诱导因子(OIF)用4M盐酸胍从牛骨有机基质中提取,并通过凝胶过滤、离子交换色谱、亲和色谱和反相高效液相色谱进行纯化。基于十二烷基硫酸钠凝胶电泳,OIF是一种表观分子量为22 - 28 kDa的糖蛋白。OIF的酶促或化学去糖基化使其质量降至约12 kDa,且活性明显丧失。在所用模型中,添加转化生长因子(TGF)-β1或TGF-β2可显著提高OIF活性,这表明TGF-β1和-2在骨再生和修复中起重要作用。OIF的N端序列与其他已报道的蛋白质无同源性。

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