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蛋白酶与碱性成纤维细胞生长因子(FGF)的共纯化

Co-purification of proteases with basic fibroblast growth factor (FGF).

作者信息

Ho P L, Carpenter M R, Smillie L B, Gambarini A G

机构信息

Departamento de Bioquímica, Universidade de São Paulo, Brasil.

出版信息

Biochem Biophys Res Commun. 1990 Jul 31;170(2):769-74. doi: 10.1016/0006-291x(90)92157-u.

Abstract

Acidic and basic fibroblast growth factors (FGFs) are proteins of 16-18 kDa. Other forms of 25-30 kDa related to this growth factor family have recently been described. All these components bind tightly to heparin-Sepharose, a property that allows the purification of several FGF-related proteins. During the purification of acidic and basic FGFs from bovine pituitary glands, we detected the presence of 28-30 kDa components that are immunoreactive against anti-basic FGF antisera. However, microsequencing analysis revealed that the 28-30 kDa components are lysosomal proteases that co-elute with basic FGF from heparin-Sepharose columns. The involvement of these proteases in the etiology of microheterogenous forms of FGFs and/or release of FGFs from the extracellular matrix is discussed.

摘要

酸性和碱性成纤维细胞生长因子(FGFs)是16 - 18 kDa的蛋白质。最近已描述了与该生长因子家族相关的25 - 30 kDa的其他形式。所有这些成分都与肝素 - 琼脂糖紧密结合,这一特性使得几种FGF相关蛋白得以纯化。在从牛垂体中纯化酸性和碱性FGFs的过程中,我们检测到存在与抗碱性FGF抗血清发生免疫反应的28 - 30 kDa成分。然而,微量测序分析表明,28 - 30 kDa成分是溶酶体蛋白酶,它们与碱性FGF从肝素 - 琼脂糖柱中共同洗脱。本文讨论了这些蛋白酶在FGFs微异质性形式的病因学和/或从细胞外基质释放FGFs过程中的作用。

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