Localization of Streptococcus mutans GS-5 glucosyltransferases and intracellular invertase.
Infect Immun
; 32(2): 830-9, 1981 May.
Article
in En
| MEDLINE
| ID: mdl-6454662
Antibodies directed against Streptococcus mutans GS-5 intracellular invertase and glucosyltransferase fractions capable of synthesizing primarily water-soluble or insoluble glucans were used to ultrastructurally localize the enzymes by means of the unlabeled antibody peroxidase-antiperoxidase method. This immunocytochemical procedure revealed that the intracellular invertase was associated primarily with the cytoplasmic membrane of the cariogenic organism. The glucosyltransferase complex responsible for insoluble glucan synthesis was localized as aggregates attached to the cell surface or extracellular polysaccharides of strain GS-5. In contrast, the glucosyltransferase activity synthesizing primarily water-soluble glucans was distributed uniformly over the cell surface or in association with extracellular polysaccharides. These results are discussed relative to the sucrose-metabolizing ability of Streptococcus mutans.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Streptococcus mutans
/
Sucrase
/
Glucosyltransferases
Language:
En
Journal:
Infect Immun
Year:
1981
Document type:
Article
Country of publication:
Estados Unidos