Co-purification of proteases with basic fibroblast growth factor (FGF).
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.
Ho
P L
PL
Departamento de Bioquímica, Universidade de São Paulo, Brasil.
Carpenter
M R
MR
Smillie
L B
LB
Gambarini
A G
AG
D000595:Amino Acid Sequence; D005346:Fibroblast Growth Factors / Q000302:isolation & purification*; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000235:genetics / Q000302:isolation & purification*; D010902:Pituitary Gland / Q000032:analysis* / Q000201:enzymology; D012689:Sequence Homology, Nucleic Acid
D005346:Fibroblast Growth Factors; D010447:Peptide Hydrolases