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- W1997320506 abstract "Potato acid phosphatase (EC 3.1.3.2) was used to remove the eight phosphate groups from αs1-casein. Unlike most acid phosphatases, which are active at pH 6.0 or below, potato acid phosphatase can catalyze the dephosphorylation of αs1-casein at pH 7.0. Although phosphate inhibition is considerable (KI = 0.42 mM phosphate), the phosphate ions produced by the dephosphorylation of casein can be removed by dialysis, allowing the reaction to go to completion. The dephosphorylated αs1-casein is homogeneous on gel electrophoresis with a slower mobility than native αs1-casein and has an amino acid composition which is identical to native αs1-casein. Thus the removal of phosphate groups from casein does not alter its primary structure. Potato acid phosphatase also removed the phosphate groups from other phosphoproteins, such as, β-casein, riboflavin binding protein, pepsinogen, ovalbumin, and phosvitin." @default.
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- W1997320506 date "1976-04-01" @default.
- W1997320506 modified "2023-10-16" @default.
- W1997320506 title "Removal of phosphate groups from casein with potato acid phosphatase" @default.
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- W1997320506 doi "https://doi.org/10.1016/0005-2744(76)90293-x" @default.
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