title: Partial purification and characterization of a putative prohormone-processing enzyme complex from bovine pituitary.
abstract: A putative prohormone-processing enzyme complex with specificity toward basic residues was partially purified from whole bovine pituitary glands. The complex is basic, binding to S-Sepharose at pH 8.2. The pH optimum of the enzyme is around 8.0. The enzyme is capable of cleaving proenkephalin and is present in at least three forms with relative molecular masses of about 36,000, 58,000, and 90,000 Da. The proteinase complex is inhibited by soybean trypsin inhibitor, limabean trypsin inhibitor, and aprotinin, but not by inhibitors of thiol proteinases or metal chelators. Our results indicate that this proteinase is a trypsin-like serine esterase with properties appropriate to that of a prohormone-processing enzyme.
authors.affiliation: Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, New Orleans 70112.
authors.forename: J W
authors.initials: JW
authors.lastname: Irvine
authors.forename: I
authors.initials: I
authors.lastname: Lindberg
mesh_terms: D000818:Animals; D002417:Cattle; D005591:Chemical Fractionation; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D006728:Hormones / Q000378:metabolism*; D008722:Methods; D008970:Molecular Weight; D010902:Pituitary Gland / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology
chemical_list: D006728:Hormones; D011480:Protease Inhibitors