PMID: 39674Sep 1, 1979

The purification and properties of dextransucrase from Streptococcus sanguis ATCC 10558

Carbohydrate Research
S HuangR M Mayer

Abstract

Dextransucrase has been purified from the culture fluids of S. sanguis 10558 by a combination of hydroxylapatite, ion-exchange, and gel-filtration steps. Two active proteins were isolated with specific activities approaching one order of magnitude higher than other preparations reported. The enzymes have mol. wt. on the order of 100 000 and exhibit pH optima between 5,8 and 6.2. In addition, detailed analysis of one of the enzymes indicates that the enzyme undergoes two ionizations that are important for activity. One pK is at 4.4 and the second at 7.4. The structures of dextrans produced by the two enzymes have been examined by p.m.r. spectroscopy, and a substantial degree of similarity was observed, with only minor differences in the proportion of alpha-(1 leads to 3) and alpha-(1 leads to 6) bonds. No evidence could be obtained that either of the enzymes was capable of catalyzing a rearrangement of alpha-(1 leads to 6) to alpha-(1 leads to 3) bonds.

References

Sep 16, 1983·Carbohydrate Research·V K ParnaikR M Mayer
Sep 16, 1983·Carbohydrate Research·G A LuzioR M Mayer
Jan 15, 1986·Biochimica Et Biophysica Acta·A W Miller, J F Robyt
Jun 1, 1992·Oral Microbiology and Immunology·M Smorawinska, H K Kuramitsu
Apr 15, 1981·Archives of Biochemistry and Biophysics·R M MayerS M Jung
Apr 15, 1981·Archives of Biochemistry and Biophysics·S M Jung, R M Mayer

Related Concepts

Filtration
Study, Methodological
Enzymes, antithrombotic
Enzymes for Treatment of Wounds and Ulcers
Body Fluids
Purification Aspects
Dextrans
Glucosyltransferases
Body Fluids and Substances
Spectrum Analysis

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