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.
Wheat Invertases: Characterization of Cell Wall-Bound and Soluble Forms
Hari B. Krishnan, Joan T. Blanchette and Thomas W. Okita
Vol. 78, No. 2 (Jun., 1985), pp. 241-245
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/4269318
Page Count: 5
You can always find the topics here!Topics: Enzymes, Cell walls, Coleoptiles, Enzyme activity, Plants, Radishes, Seedlings, Gels, Sodium, pH
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
Wheat coleoptiles have two distinct invertases, a soluble and a cell wall-bound form as indicated by results from cytochemical and biochemical studies. These enzyme activities differ in their pH optima, chromatographic behavior on diethylaminoethyl cellulose, kinetic properties, thermal stability, and response to light treatment. The soluble invertase was purified to near homogeneity by diethylaminoethyl-cellulose, concanavalin-A Sepharose, and Sephacryl S-300 chromatography. The overall purification was 175-fold with a recovery of about 26%. The holoenzyme has an apparent molecular weight of 158,000 and subunit molecular weight of 53,000 as estimated by polyacrylamide gel electrophoresis under denaturing conditions. Illumination of wheat seedlings caused an increase in the cell wall, but not the soluble, invertase activity.
Plant Physiology © 1985 American Society of Plant Biologists (ASPB)