Purification, and comparison, of two forms of dextransucrase from Streptococcus sanguis.
A procedure has been developed whereby native and proteolyzed forms of dextransucrase have been purified; it involves gel filtration, and hydroxylapatite chromatography in the presence of 0.10% sodium dodecyl sulfate. This procedure is highly reproducible, and permits approximately 30% recovery of high purity (94% homogeneous) enzyme as an inactive, SDS complex that can be reactivated by the addition of Triton X-100. The purified enzymes have been compared with regard to amino acid compositions, and isoelectric and catalytic properties. An analysis of the structure of their product D-glucans was also made. Although the structural characteristics of the enzyme forms differ, proteolysis does not cause alterations in their catalytic properties.
Grahame
D A
DA
Mayer
R M
RM
D000596:Amino Acids / Q000032:analysis; D005964:Glucosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D013298:Streptococcus sanguis / Q000201:enzymology*
D000596:Amino Acids; D005964:Glucosyltransferases; C020025:dextransucrase