Elizabeth Bingham

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A casein kinase that catalyzes the phosphorylation of dephosphorylated aSI-casein by ATP has been found in the Golgi apparatus of lactating rat mammary gland. Dephosphorylated /3and K-Caseins are also phosphorylated by this enzyme, while other milk proteins (P-lactoglobulin, a-lactalbumin, native CY,~-, fi-, and K-case& and proteins of the fat globule(More)
The [Ca2+ + Mg2+]-ATPase activity of bovine lactating mammary gland is associated with membranes. This study compares the ATPase activity in microsomal membranes to that of the Golgi apparatus. The enzyme activity in both fractions hydrolyzed Ca(2+)-ATP and Mg(2+)-ATP. The ATPase activities were inhibited by p-chloromercuribenzoate, indicating the(More)
The lactating mammary gland synthesizes and secretes large amounts of phosphoproteins that mainly are associated with the casein fraction of milk. The free amino acids and inorganic phosphate of blood serve as building materials for casein, and the final product appears in milk as a colloidal-sized particle, the casein micelle. According to our present(More)
Potato acid phosphatase (EC 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(More)
Casein kinase from lactating bovine mammary gland catalyses the transfer of the terminal phosphoryl group of ATP to specific serine residues in dephosphorylated caseins. Best substrates for casein kinase are the dephosphorylated proteins (bovine alpha S1- and beta-caseins and pepsin), unphosphorylated human beta-casein and the dephosphorylated peptide(More)