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. 1986 Apr 1;235(1):265–268. doi: 10.1042/bj2350265

The presence of a Zn2+-dependent acid p-nitrophenyl phosphatase in bovine liver. Isolation and some properties.

F Panara
PMCID: PMC1146676  PMID: 3017299

Abstract

The presence of a Zn2+-dependent acid p-nitrophenyl phosphatase (EC 3.1.3.2) in bovine liver was described. The enzyme was purified to apparent homogeneity and migrates as a single band during electrophoresis on polyacrylamide gel. The enzyme requires Zn2+ ions for catalytic activity, other bivalent cations have little or no effect. The enzyme, of Mr 118,000, optimum pH 6-6.2 and pI 7.4-7.5, was inhibited by EDTA, tartrate, adenine and ATP, but not by fluoride. The common phosphate esters are poor substrates for the enzyme, which hydrolyses preferentially p-nitrophenyl phosphate and o-carboxyphenyl phosphate. The Zn2+-dependent acid p-nitrophenyl phosphatase of bovine liver was different from the high-Mr acid phosphatases previously detected in mammalian tissues.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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