Purification of NADH: Hypothiocyanite oxidoreductase in Streptococcus sanguis

被引：15

作者：

Courtois, P

Pourtois, M

机构：

[1] Laboratory of Stomatology, Faculty of Medicine, Free University of Brussels, Brussels

[2] Laboratory of Stomatology, Brussels Free University, B-1070 Brussels

来源：

BIOCHEMICAL AND MOLECULAR MEDICINE | 1996年 / 57卷 / 02期

关键词：

D O I：

10.1006/bmme.1996.0019

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：

NADH: hypothiocyanite oxidoreductase (NHOR) activity, found in some oral Streptococci, is postulated to protect these microorganisms against salivary peroxidase-produced hypothiocyanite, NHOR, however, has not been purified so far. The purification of NHOR from crude extracts of Streptococcus sanguis NCTC 7863 strain (by ultrafiltation and anion-exchange chromatography) revealed one fraction of 125 +/- 1 kDa. However, SDS-PAGE electrophoresis provided a single protein of 21.1 +/- 1.2 kDa, This last discovery suggests that NHOR enzyme is a hexameric complex having six subunits. (C) 1996 Academic Press, Inc.

引用

页码：134 / 138

页数：5

共 13 条

[1] ACCUMULATION OF HYPOTHIOCYANITE ION DURING PEROXIDASE-CATALYZED OXIDATION OF THIOCYANATE ION [J].