JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Harsanyi, Z.
Right arrow Articles by Dorn, G. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Harsanyi, Z.
Right arrow Articles by Dorn, G. L.

 Previous Article  |  Next Article 

J Bacteriol. 1972 April; 110(1): 246-255
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Purification and Characterization of Acid Phosphatase V from Aspergillus nidulans

Zsolt Harsanyi1 and Gordon L. Dorn

Department of Genetics, Albert Einstein College of Medicine, New York, New York 10461
Department of Microbiology, Wadley Institutes of Molecular Medicine, Dallas, Texas 75246

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.

FOOTNOTES

1 Present address: Department of Microbiology, Cornell University Medical College, New York, N.Y. 10021.

J Bacteriol. 1972 April; 110(1): 246-255
Copyright © 1972 American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1972 by the American Society for Microbiology. All rights reserved.