Abstract
A convenient and rapid method for the purification of Streptococcus mutans dextransucrase is described. Affinity chromatography, on a column containing insoluble dextran purified from a culture of S. mutans 6715-49, gave an almost 300-fold purification, with 76% recovery of enzyme. Subsequent hydrophobic chromatography on butyl-agarose increased the overall enzyme purification to more than 1,000-fold, with a 65% recovery of activity. Two components of the dextransucrase activity were separated during hydrophobic chromatography. Both synthesized insoluble glucan as their major product and were capable of synthesizing soluble glucan in the presence of exogenous soluble dextran. However, the major enzyme component, which coeluted with a catalytically inert, dextran-binding protein, was greatly stimulated by exogenous soluble dextran, whereas the second enzyme component was not.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Reference16 articles.
1. Purification and properties of dextransucrase from Streptococcus mutans;Chludzinski A. M.;J. Bacteriol.,1974
2. Multicomponent nature of the glucosyltransferase system of Streptococcus mutans;Ciardi J. E.;J. Dent. Res. 55(Special Issue C):C87-C96.,1976
3. Disc electrophoresis. II. Method and application to human serum proteins;Davis B. J.;Ann. N. Y. Acad. Sci.,1964
4. Purification and properties of dextransucrase and invertase from Streptococcus mutans;Fukui L.;J. Bacteriol.,1974
5. Determination of enzymatic activity in polyacrylamide gels. I. Enzymes catalyzing the conversion of non-reducing substrates to reducing products;Gabriel O.;Anal. Biochem.,1969
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