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Purification of myo-Inositol l-Phosphate Synthase from Rice Cell Culture by Affinity Chromatography

Edward A. Funkhouser and Frank A. Loewus
Plant Physiology
Vol. 56, No. 6 (Dec., 1975), pp. 786-790
Stable URL: http://www.jstor.org/stable/4264259
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Purification of myo-Inositol l-Phosphate Synthase from Rice Cell Culture by Affinity Chromatography
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Abstract

myo-Inositol 1-phosphate synthase (EC 5.5.1.4) is the enzyme which catalyzes the synthesis of the precursor for the myo-inositol oxidation pathway. Rice callus grown in suspension culture provides a good source of plant enzyme. Use has been made of a noncompetitive inhibitor to prepare an affinity column for this enzyme. With this column, the enzyme from rice callus has been purified 1500-fold in a single step, about 9000-fold over-all, to a specific activity of 0.078 units per milligram of protein. This is an order of magnitude greater than previous purifications of the plant enzyme.

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