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. 1974 Feb;117(2):667–674. doi: 10.1128/jb.117.2.667-674.1974

β-d-Phosphogalactoside Galactohydrolase from Streptococcus cremoris HP: Purification and Enzyme Properties1

K G Johnson a, I J McDonald a
PMCID: PMC285558  PMID: 4204438

Abstract

β-d-phosphogalactoside galactohydrolase (β-PGal) was isolated and purified from cell-free extracts of Streptococcus cremoris HP to apparent homogeneity to gel electrophoresis. Using the chromogenic o-nitrophenol-β-d-galactopyranoside-6-phosphate as substrate, the purified enzyme exhibited a specific activity of 18.71 U/mg of protein and Km and Vmax values of 5.88 × 10−4 M and 23.8 μmol of o-nitrophenol liberated per min per mg of protein, respectively. d-Galactose-6-phosphate was a weak competitive inhibitor of β-PGal. Activity was relatively heat resistant and was maximal from pH 5.0 to 8.0 and over a temperature range of 45 to 52 C. Dithiothreitol, ethylenediaminetetraacetic acid, and citrate stimulated β-PGal activity, whereas Mg2+, Li1+, and p-hydroxymercuribenzoate were inhibitory. Molecular weight of the enzyme was estimated at 6.76 × 104. Amino acid composition was similar to other β-phosphogalactosidases previously investigated, with the exception that the S. cremoris enzyme contains a small amount of half cystine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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