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- W2364955023 abstract "Inhibition by thiamin of yeast“acid”phosphatase was noticeable at a concentration of 3×10~(-5)M,and reached a maximum at 3×10~(-4)M.On further increasing the concentration of thiamin,there was no corresponding increase in the extent of inhibition. Maximum inhibition was attained at different levels of residual activity, depending upon the substrate used.Withβ-glycerophosphate as substrate, maximum inhibition of over 50% was obtained,while with phenylphosphate, it was only about 30%. Thiamin was also found to shift the optimum pH of the enzyme.With 0.005 M phenylphosphate as substrate,the optimum pH dropped from 3.40 to 3.25.Inhibition was observed only on the alkaline side of the shifted optimum,being practically non-existent on the acid side. Thiamin inhibition was demonstrated to be completely reversible by dialysis against distilled water. From a study of the chemical kinetics of the enzyme,it was concluded that the inhibition by thiamin was essentially non-competitive in nature. 2-methyl-5-cyano-6-amino-pyrimidine,a compound similar in structure to the pyrimidine moiety of the thiamin molecule,was also found to be an inhibitor of yeast“acid”phosphatase.Maximum inhibition also occurred at 3×10~(-4)M,but the extent of inhibition at the maximum was much less, being only 14% when phenylphosphate was the substrate." @default.
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- W2364955023 date "1954-03-01" @default.
- W2364955023 modified "2023-10-17" @default.
- W2364955023 title "The effect of thiamin on yeast acid phosphatase." @default.
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