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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. The Pasteurella haemolytica O-sialoglycoprotein endopeptidase is inhibited by zinc ions and does not cleave fetuin. Cladman, W.M., Watt, M.A., Dini, J.P., Mellors, A. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
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