Purification and subcellular localization of Zn-dependent acid p-nitrophenylphosphatase in frog liver and comparison with other vertebrates.
Zn2(+)-dependent acid p-nitrophenylphosphatase (Zn-AcPase) from liver of Rana esculenta was purified to homogeneity. The purified enzyme moves as a single electrophoretic band at pH 8.3 in 7.5% acrylamide and was coincident with the enzyme activity. The enzyme has a molecular weight of 102,000 +/- 5,000D and is a dimer with two apparently similar polypeptide chains of 48,000 +/- 3,000D as determined by sodium dodecylsulfate gel electrophoresis. Zn-AcPase from frog liver requires Zn2+ ions for catalytic activity; other bivalent cations have little or no effect. The enzyme with a pI of 7.07 does not appear to be a glycoprotein and was associated with the soluble fraction after liver cell fractionation. The biochemical and molecular properties of frog liver Zn-AcPase were compared with that of the enzyme partially purified from carp (Cyprinus carpio), pike (Esox lucius), and rat (Rattus norvegicus).
Panara
F
F
Istituto di Biologia Cellulare, Universita' di Perugia, Italy.
Massetti
N
N
Angiolillo
A
A
Fagotti
A
A
Pascolini
R
R
D009597:4-Nitrophenylphosphatase / Q000302:isolation & purification*; D000818:Animals; D002347:Carps / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D011893:Rana esculenta / Q000378:metabolism*; D051381:Rats; D012487:Salmonidae / Q000378:metabolism; D014714:Vertebrates / Q000378:metabolism*; D015032:Zinc / Q000502:physiology*
D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D015032:Zinc