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. 1972 Apr;110(1):246–255. doi: 10.1128/jb.110.1.246-255.1972

Purification and Characterization of Acid Phosphatase V from Aspergillus nidulans

Zsolt Harsanyi 1,2,1, Gordon L Dorn 1,2
PMCID: PMC247404  PMID: 4552990

Abstract

Acid phosphatase V of Aspergillus nidulans was purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The enzyme demonstrated a charge microheterogeneity on starch and acrylamide gel electrophoresis, but proved to be homogeneous on ultracentrifugation and gel filtration. Phosphatase V was found to be a classic acid orthophosphoric monoester phosphohydrolase, and it cleaved p-nitrophenylphosphate, glucose-6-phosphate, and uridine-5′-monophosphate at maximal rates. It was inhibited by fluoride, borate, and molybdate ions, and demonstrated end-product inhibition by inorganic phosphate. Metallic ions or cofactors were not required for activity. The molecular weight was estimated to be 100,000, the S20,w was calculated to be 4.1, and the pH optimum was found to be 6.1.

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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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