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- W1517755719 abstract "Abstract Choline kinase was purified approximately 300-fold, in 5% yield, from an autolysate of dried brewers' yeast. A molecular weight of 67,000 was estimated using a Stokes radius of 33 A, as determined by Sephadex G-200 chromatography. An s20,w of 4.8 S was obtained by sucrose density gradient centrifugation. Enzyme activity was diminished by sulfhydryl inhibitors and stabilized by the presence of magnesium ion. The Michaelis constant for ATP was 1.4 x 10-4 m. The Michaelis constant with respect to choline was 1.5 x 10-5 m at low choline concentrations; reciprocal plots at high choline concentrations were non-linear. Initial velocity and product and dead-end inhibitor studies were performed on the forward reaction and were consistent with a Random Bi-Bi mechanism for catalysis." @default.
- W1517755719 created "2016-06-24" @default.
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- W1517755719 date "1973-04-01" @default.
- W1517755719 modified "2023-09-26" @default.
- W1517755719 title "Choline Kinase from Brewers' Yeast" @default.
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- W1517755719 doi "https://doi.org/10.1016/s0021-9258(19)44118-5" @default.
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