title: Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum.
abstract: The rates of folding and disulfide bond formation in reduced BPTI were measured in vitro in the presence and absence of total protein from the endoplasmic reticulum. The rates were increased substantially by the endoplasmic reticulum proteins, but only to the extent expected from the known content and activity of protein-disulfide-isomerase. No effects of added ATP or Ca2+ were observed, even though protein-disulfide-isomerase binds Ca2+ tightly.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, England, United Kingdom.
authors.forename: A
authors.initials: A
authors.lastname: Zapun
authors.forename: T E
authors.initials: TE
authors.lastname: Creighton
authors.forename: P J
authors.initials: PJ
authors.lastname: Rowling
authors.forename: R B
authors.initials: RB
authors.lastname: Freedman
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D007611:Aprotinin / Q000737:chemistry*; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D004721:Endoplasmic Reticulum / Q000737:chemistry / Q000502:physiology*; D008565:Membrane Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D051379:Mice; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins; D000255:Adenosine Triphosphate; D007611:Aprotinin; D002118:Calcium