This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Maynard, M T Articles by Kuramitsu, H K Search for Related Content PubMed PubMed Citation Articles by Maynard, M T Articles by Kuramitsu, H K

 Previous Article  |  Next Article 

Infect Immun. 1979 March; 23(3): 873-883

Purification and antigenic properties of intracellular invertase from Streptococcus mutans.

ABSTRACT

Intracellular invertase from Streptococcus mutans GS5 was purified to near homogeneity by gel filtration and ion-exchange chromatography followed by preparative polyacrylamide gel electrophoresis. The invertase appeared to be composed of a single polypeptide chain with a molecular weight of 48,000. Extracellular invertase was identified in strain GS5 and was determined to have a molecular weight of 500,000. No antigenic relationship between these two forms of invertase was observed since antibody prepared against purified intracellular invertase neither affected extracellular invertase activity nor precipitated that enzyme on immunodiffusion. No antigenic relatedness between intracellular invertase and glucosyl- and fructosyl- transferases was detected since cross-reactivity with antibody prepared against either enzyme fraction was not observed after immunodiffusion. Using immunodiffusion and quantitative precipitin data, we examined the relationships of other S. mutans intracellular invertases to the serotype c enzyme. It appeared that the intracellular invertases from serotypes e, f, and g were structurally similar to the enzyme from serotype c, whereas the structure of invertases from serotypes a, b, and d appeared less similar to that of enzyme from serotype c.