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The Disulfide Structure of Bovine Pituitary Basic Fibroblast Growth Factor

The Disulfide Structure of Bovine Pituitary Basic Fibroblast Growth Factor

S A Thompson

J Biol Chem. 1992 Feb 5;267(4):2269-73.

PMID: 1733934

Abstract:

Basic fibroblast growth factor has 4 cysteine residues in its amino acid sequence, two of which are perfectly conserved within the fibroblast growth factor family of proteins suggesting a disulfide bond at this position. Furthermore, thiol titration of bovine pituitary basic fibroblast growth factor (bFGF) indicates the presence of two free thiols, which is consistent with an intramolecular disulfide. Direct analysis of natural and recombinant fibroblast growth factor proteins have not confirmed the existence of such a disulfide. Instead, the two nonconserved cysteines of bFGF purified from bovine pituitaries are S-thiolated with glutathione. Inclusion of 75 mM N-ethylmaleimide during the homogenization of the pituitaries effectively blocks the S-thiolation, demonstrating that this modification is an artifact of the purification procedure. Analysis of the N-ethylmaleimide purified bovine pituitary bFGF suggests that the natural protein is in the correct redox state when all 4 cysteines are in the reduced form.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP106096939-A	Fibroblast Growth Factor-Basic from bovine pituitary		106096-93-9	Price

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