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- W1628726261 abstract "Constitutive β-glucosidases from Saccharomyces fragilis (Y-18) and S. dobzhanskii (Y-19) precipitated at the same concentration of ammonium sulfate. The partially purified enzymes had similar activation energies, molecular weights, affinities for certain natural and synthetic β-glucosides, and optimal p H values for substrate hydrolysis, and they were stable over approximately the same p H range. The enzymes, however, could be clearly distinguished by other criteria. Affinities of the synthetic, sulfur-containing β-glucosides for Y-18 enzyme were many times greater than for Y-19 enzyme. The latter enzyme was more resistant to heat. The two enzymes eluted from diethylaminoethyl cellulose at different concentrations of sodium chloride. In precipitin tests, homologous enzyme-antisera systems were highly specific. The β-glucosidase synthesized by a hybrid, S. fragilis × S. dobzhanskii (Y-42), was unique. Characterization of this enzyme produced values which were intermediate to those for the enzymes from the parental yeast strains. Heat-inactivation slopes and Lineweaver-Burk plots for the Y-42 enzyme were anomalous. It is suggested that hydrolytic activity in Y-42 preparations is due to a spectrum of hybrid enzyme molecules composed of varying amounts of two distinct polypeptides. It is further suggested that these polypeptides may be identical to those synthesized by the parental Y-18 and Y-19 yeast strains." @default.
- W1628726261 created "2016-06-24" @default.
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- W1628726261 date "1967-01-01" @default.
- W1628726261 modified "2023-09-22" @default.
- W1628726261 title "Purification and Characterization of Yeast β-Glucosidases" @default.
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- W1628726261 doi "https://doi.org/10.1128/jb.93.1.135-141.1967" @default.
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