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

被引：8
作者：
Cladman, WM
Watt, MAV
Dini, JP
Mellors, A
机构：
[1] Guelph-Waterloo Ctr. Grad. Wk. Chem., Dept. of Chemistry and Biochemistry, University of Guelph, Guelph
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 220卷 / 01期
关键词：
D O I：
10.1006/bbrc.1996.0371
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 1996 Academic Press, Inc.
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页码：141 / 146
页数：6
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