Glycosyltransferases of Streptococcus mutans strain Ingbritt.
The glycosyltransferases of S. mutans strain Ingbritt have been resolved by SDS-polyacrylamide gel electrophoresis, followed by incubation in the presence of non-ionic detergent to restore enzyme activity. A group of high molecular weight proteins synthesizing glucans has been identified, as well as three distinct fructan-synthesizing activities. The glucan-forming enzymes have been purified by affinity chromatography on insoluble glucan, followed by gel chromatography in SDS, and antiserum to the purified enzymes has shown that they are antigenically identical within serotypes c, e and f, and cross-react strongly with serotype b.
D000942:Antigens, Bacterial / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005630:Fructans / Q000096:biosynthesis; D005936:Glucans / Q000096:biosynthesis; D005964:Glucosyltransferases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D005779:Immunodiffusion; D007123:Immunoelectrophoresis, Two-Dimensional; D008970:Molecular Weight; D013295:Streptococcus mutans / Q000201:enzymology*
D000942:Antigens, Bacterial; D005630:Fructans; D005936:Glucans; D005964:Glucosyltransferases