| pubmed-article:2950996 | pubmed:abstractText | A simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans. | lld:pubmed |
