Removal of phosphate groups from casein with potato acid phosphatase.

Biochimica et biophysica acta (1976-04-08)
E W Bingham, H M Farrell
PMID4132
RESUMO

Potato acid phosphatase (EC 3.1.3.2) was used to remove the eight phosphate groups from alphas1-casein. Unlike most acid phosphatases, which are active at pH 6.0 or below, potato acid phosphatase can catalyze the dephosphorylation of alphas1-casein at pH 7.0. Although phosphate inhibition is considerable (K1=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 alphas1-casein is homogeneous on gel electrophoresis with a slower mobility than native alphas1-casein and has an amino acid composition which is identical to native alphas1-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 beta-casein, riboflavin binding protein, pepsinogen, ovalbumin, and phosvitin.

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Roche
Acid Phosphatase, grade II, from potato
Sigma-Aldrich
Phosphatase, Acid from potato, lyophilized powder, ≥3.0 units/mg solid
Sigma-Aldrich
Phosphatase, Acid from potato, Suitable for manufacturing of diagnostic kits and reagents