Purification of myo-Inositol 1-Phosphate Synthase from Rice Cell Culture by Affinity Chromatography | Zendy

Edward Funkhouser | Zendy; Frank A. Loewus | Zendy

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Purification of myo-Inositol 1-Phosphate Synthase from Rice Cell Culture by Affinity Chromatography

Author(s) -

Edward Funkhouser,

Frank A. Loewus

Publication year - 1975

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.56.6.786

Subject(s) - enzyme , callus , biochemistry , phosphate , atp synthase , enzyme assay , biology , affinity chromatography , cell culture , botany , genetics

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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