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Wheat Invertases: Characterization of Cell Wall-Bound and Soluble Forms

Hari B. Krishnan, Joan T. Blanchette and Thomas W. Okita
Plant Physiology
Vol. 78, No. 2 (Jun., 1985), pp. 241-245
Stable URL: http://www.jstor.org/stable/4269318
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.
Wheat Invertases: Characterization of Cell Wall-Bound and Soluble Forms
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Abstract

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.

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