Purification and characterisation of the extracellular d-glucosyltransferase from serotype c Streptococcus mutans
| Autor: | Tomonari Ogawa, Shigeyuki Hamada, Tadashi Baba, Motoi Morimoto, Tsuyoshi Yakushiji, Nobuo Okahashi, Toshihiko Koga |
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| Rok vydání: | 1986 |
| Předmět: |
Serotype
Biochemistry Substrate Specificity Analytical Chemistry Microbiology Streptococcus mutans chemistry.chemical_compound Glycosyltransferase Extracellular Amino Acids chemistry.chemical_classification biology Organic Chemistry General Medicine biology.organism_classification Molecular Weight Kinetics Isoelectric point Enzyme Dextran chemistry Glucosyltransferases biology.protein Bacteria |
| Zdroj: | Carbohydrate Research. 158:147-155 |
| ISSN: | 0008-6215 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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