title: The Pasteurella haemolytica O-sialoglycoprotein endopeptidase is inhibited by zinc ions and does not cleave fetuin.
abstract: Culture supernatants of Pasteurella haemolytica A1 contain an O-sialoglycoprotein endopeptidase that cleaves human glycophorin A. This enzyme is inhibited by micromolar concentrations of Zn2+. It can be separated from a neuraminidase activity in culture supernatants by ion-exchange chromatography. The neuraminidase activity can cause the de-sialation of the bovine soluble sialoglycoprotein, fetuin. However fetuin is not cleaved proteolytically either by culture supernatants from P. haemolytica A1 or by chromatographically purified O- sialoglycoprotein endopeptidase or neuraminidase.
authors.affiliation: Guelph-Waterloo Centre for Graduate Work in Chemistry, University of Guelph, Ontario N1G 2W1, Canada.
authors.forename: W M
authors.initials: WM
authors.lastname: Cladman
authors.forename: M A
authors.initials: MA
authors.lastname: Watt
authors.forename: J P
authors.initials: JP
authors.lastname: Dini
authors.forename: A
authors.initials: A
authors.lastname: Mellors
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D002417:Cattle; D006021:Glycophorins; D006801:Humans; D066298:In Vitro Techniques; D016978:Mannheimia haemolytica / Q000201:enzymology* / Q000235:genetics; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D015032:Zinc / Q000494:pharmacology; D000509:alpha-Fetoproteins
chemical_list: D006021:Glycophorins; D000509:alpha-Fetoproteins; D008666:Metalloendopeptidases; C070738:O-sialoglycoprotein endopeptidase; D015032:Zinc