title: Furin cleavage of bacterial expressed glutathione-S-transferase-pro-transforming growth factor beta1 fusion protein in vitro.
abstract: To investigate the processing of transforming growth factor beta1 (TGFbeta1) pro-protein by furin protease we expressed a GST-pro-TGFbeta1 fusion protein in bacteria. Analysis of the furin digestion pattern revealed the liberation of 12.5 kDa TGFbeta1 monomers. There was no evidence for cleavage of an alternative furin site within the pro-protein.
authors: Dr. Margarete Fischer-Bosch Institute of Clinical Pharmacology, Robert Bosch Hospital, 70376 Stuttgart, Germany.
authors: N A
authors: NA
authors: Kahle
authors: C
authors: C
authors: Joffroy
authors: S L
authors: SL
authors: Popp
authors: C
authors: C
authors: Knabbe
authors: M B
authors: MB
authors: Stope
mesh_terms: D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D045683:Furin / Q000378:metabolism*; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D053773:Transforming Growth Factor beta1 / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D011993:Recombinant Fusion Proteins; D053773:Transforming Growth Factor beta1; D005982:Glutathione Transferase; D045683:Furin