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
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.
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页码:769 / 774
页数:6
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