Purification and subcellular localization of Zn-dependent acidp-nitrophenylphosphatase in frog liver and comparison with other vertebrates
✍ Scribed by Panara, F. ;Massetti, N. ;Angiolillo, A. ;Fagotti, A. ;Pascolini, R.
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 729 KB
- Volume
- 254
- Category
- Article
- ISSN
- 0022-104X
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✦ Synopsis
Abstract
Zn^2+^‐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 Zn^2+^ 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).