Pituitary fibroblast growth factors: immunocharacterization of an acid component and N-terminal sequence analysis of a truncated basic component.
Extraction of bovine pituitaries at pH 7.0, in the presence or absence of protease inhibitors (PMSF, leupeptin, pepstatin A and EDTA) yielded both basic and acidic FGF components that were characterized by Western blotting and sequence analysis. Basic FGF comprised several components: an 18 KDa form that is similar, if not identical, to the basic FGF (1-146) already described; a 17 KDa form that is likely to be a new truncated molecular species (11-146) and a group of immunoreactive components of about 29 KDa. Acidic FGF showed several active components of pI 4.5-6.5. The most active component has a pI of approximately 5.0; molecular weight of 17 KDa and is shown, by Western blotting, to be similar to a truncated form of bovine brain acidic FGF. The biological activity of the latter component is shown to be neutralized by anti-brain acidic FGF antiserum.
Ho
P L
PL
Departmento de Bioquimica, Universidade de São Paulo, Brasil.
Jakes
R
R
Northrop
F D
FD
Gambarini
A G
AG
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002846:Chromatography, Affinity; D005346:Fibroblast Growth Factors / Q000276:immunology / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D010902:Pituitary Gland / Q000032:analysis*; D012685:Sepharose
D000596:Amino Acids; D005346:Fibroblast Growth Factors; D012685:Sepharose