Separation and some properties of two acid phosphatases from suspension cultures ofIpomoea sp. |
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| Authors: | M W Zink I A Veliky |
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| Institution: | (1) Department of Biology, University of Saskatchewan, S7N OW0 Saskatoon, Canada;(2) Division of Biological Sciences, National Research Council of Canada, K1A OR6 Ottawa, Canada |
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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.
Issued as NRCC No. 20658 |
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| Keywords: | Ipomoea morning glory cell culture acid phosphatases |
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