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Separation and some properties of two acid phosphatases from suspension cultures ofIpomoea sp.

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Abstract

Two acid phosphatases isolated from culturedIpomoea (moring glory) cells were separated by column chromatography on DEAE-cellulose. The two acid phosphatases have different pH optima (pH 4.8–5.0 and 6.0) and do not require the presence of divalent ions. The enzymes possess high activity toward pyrophosphate,p-nitrophenylphosphate, nucleoside di- and triphosphates, and much less activity toward nucleoside monophosphates and sugar esters. The two phosphatases differ from each other in Michaelis constants, in the degree of inhibition by arsenate, fluoride and phosphate and have quantitative differences of substrate specificity. In addition, they also differ in their response to various ions.

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Authors and Affiliations

  1. Department of Biology, University of Saskatchewan, S7N OW0, Saskatoon, Canada

    M. W. Zink

  2. Division of Biological Sciences, National Research Council of Canada, K1A OR6, Ottawa, Canada

    I. A. Veliky

Authors
  1. M. W. Zink
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  2. I. A. Veliky
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Issued as NRCC No. 20658

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Zink, M.W., Veliky, I.A. Separation and some properties of two acid phosphatases from suspension cultures ofIpomoea sp.. Plant Cell Tiss Organ Cult 1, 265–273 (1981). https://doi.org/10.1007/BF02318923

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  • DOI: https://doi.org/10.1007/BF02318923

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