@article{mbs:/content/journal/micro/10.1099/00221287-133-5-1351, author = "Hanada, Nobuhiro and Takehara, Tadamichi and Saeki, Eiichi", title = "Purification and Characterization of a Third Glucosyltransferase from Streptococcus Mutans Serotype g", journal= "Microbiology", year = "1987", volume = "133", number = "5", pages = "1351-1358", doi = "https://doi.org/10.1099/00221287-133-5-1351", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-133-5-1351", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "SUMMARY: Streptococcus mutans strain AHT (serotype g) secretes at least two glucosyltransferases with different pI values. A novel glucosyltransferase with a pI of 5·8 was purified 244-fold from the ammonium sulphate fraction by DEAE-cellulose chromatography, FPLC (Mono Q column, Pharmacia) and hydrophobic chromatography. The enzyme preparation gave a single protein band on analysis by both PAGE and SDS-PAGE, and did not form multiple protein bands detectable by IEF. The M r was estimated to be about 130000 by SDS-PAGE and about 135000 by ultracentrifugal analysis. The apparent K m value and pH optimum of the enzyme were 3·9 ± 0·2 mm (mean ± sd) and about 4·7, respectively. The enzyme synthesized water-soluble glucan from sucrose, and the glucan consisted of over 90 mol% 1,6-α-d-glucosidic linkages. The enzyme activity was not stimulated by primer dextran. Anti-enzyme serum produced a single precipitin band with the purified enzyme preparation, whereas it did not react with either of the other two known glucosyltransferases.", }