Literature DB >> 8602834

The Pasteurella haemolytica O-sialoglycoprotein endopeptidase is inhibited by zinc ions and does not cleave fetuin.

W M Cladman1, M A Watt, J P Dini, A Mellors.   

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.

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Year:  1996        PMID: 8602834     DOI: 10.1006/bbrc.1996.0371

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

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Authors:  Heinz Läubli; Frederico Alisson-Silva; Michal A Stanczak; Shoib S Siddiqui; Liwen Deng; Andrea Verhagen; Nissi Varki; Ajit Varki
Journal:  J Biol Chem       Date:  2014-10-15       Impact factor: 5.157

2.  Expression and protease characterization of a conserved protein YgjD in Vibrio harveyi.

Authors:  Yayuan Zhang; Jixiang Chen; Yonggang Wang; Yanlin Li; Wenhong Rui; Jiyi Zhang; Dan Luo
Journal:  PeerJ       Date:  2020-05-18       Impact factor: 2.984

3.  The Glycoprotease CpaA Secreted by Medically Relevant Acinetobacter Species Targets Multiple O-Linked Host Glycoproteins.

Authors:  M Florencia Haurat; Nichollas E Scott; Gisela Di Venanzio; Juvenal Lopez; Benjamin Pluvinage; Alisdair B Boraston; Michael J Ferracane; Mario F Feldman
Journal:  mBio       Date:  2020-10-06       Impact factor: 7.867

  3 in total

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