Purification and characterization of acid phosphatase V from Aspergillus nidulans.

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 S(20,w) was calculated to be 4.1, and the pH optimum was found to be 6.1.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Harsanyi Z,Dorn GL

doi

10.1128/JB.110.1.246-255.1972

subject

Has Abstract

pub_date

1972-04-01 00:00:00

pages

246-55

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

110

pub_type

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