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PMID: 3161832 Published · ppublish English Journal Article

Isolation and characterization of an extracellular glucosyltransferase synthesizing insoluble glucan from Streptococcus mutans serotype c.

Infection and immunity ·Vol. 49 ·No. 3 ·1985-09-00 ·Pages 790-6

Mukasa H, Tsumori H, Shimamura A

Abstract

A glucosyltransferase which synthesized insoluble glucan in polyacrylamide gel was isolated from the culture supernatant of Streptococcus mutans Ingbritt (serotype c) by ultrafiltration, ethanol fractionation, isoelectric focusing, and preparative gel electrophoresis. The enzyme preparation was electrophoretically homogeneous and immunologically distinct from the highly branched 1,6-alpha-D-glucan synthase and fructosyltransferase from the same strain and glucosyltransferases from serotypes a and g. The molecular weight was 99,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the isoelectric point was 8.5. The enzyme had the optimum pH of 6.0 and Km value for sucrose of 9.4 mM. Besides the insoluble glucan with 96% 1,3-alpha linkage, this enzyme synthesized a considerable amount of diffusible glucan with 84% 1,6-alpha linkage, separately. This enzyme may be the one released from the enzyme aggregates by extracellular proteases, because the addition of extraneous trypsin to the crude enzyme preparation increased the amount of the enzyme species.

MeSH Terms
Animals Electrophoresis, Polyacrylamide Gel Glucans/biosynthesis Glucosyltransferases/analysis,immunology,isolation & purification Kinetics Rabbits Streptococcus mutans/enzymology
Chemicals
Glucans Glucosyltransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mukasa H
Tsumori H
Shimamura A
References (39)
39 references, click to expand
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
1985-09-00
Pages
790-6
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC261278
Subset
IM
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