The Pasteurella haemolytica O-sialoglycoprotein endopeptidase is inhibited by zinc ions and does not cleave fetuin.
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.
Cladman
W M
WM
Guelph-Waterloo Centre for Graduate Work in Chemistry, University of Guelph, Ontario N1G 2W1, Canada.
Watt
M A
MA
Dini
J P
JP
Mellors
A
A
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
D006021:Glycophorins; D000509:alpha-Fetoproteins; D008666:Metalloendopeptidases; C070738:O-sialoglycoprotein endopeptidase; D015032:Zinc