COPURIFICATION OF PROTEASES WITH BASIC FIBROBLAST GROWTH-FACTOR (FGF)

被引：5

作者：

HO, PL ^{[1
]}

CARPENTER, MR ^{[1
]}

SMILLIE, LB ^{[1
]}

GAMBARINI, AG ^{[1
]}

机构：

[1] UNIV ALBERTA, DEPT BIOCHEM, MRC, PROT STRUCT & FUNCT GRP, EDMONTON T6G 2H7, ALBERTA, CANADA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 170卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92157-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 antibasic 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. © 1990.

引用

页码：769 / 774

页数：6