You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. 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
Edward A. Funkhouser and Frank A. Loewus
Vol. 56, No. 6 (Dec., 1975), pp. 786-790
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/4264259
Page Count: 5
You can always find the topics here!Topics: Enzymes, Plants, Callus, Chromatography, Rice, Inositols, Biosynthesis, Testes, Cell growth, Cell culture techniques
Were these topics helpful?See somethings inaccurate? Let us know!
Select the topics that are inaccurate.
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.
Preview not available
myo-Inositol 1-phosphate synthase (EC 18.104.22.168) 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.
Plant Physiology © 1975 American Society of Plant Biologists (ASPB)