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Plant Physiology 78:241-245 (1985)
© 1985 American Society of Plant Biologists

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Articles

Wheat Invertases 1

Characterization of Cell Wall-Bound and Soluble Forms

Hari B. Krishnan, Joan T. Blanchette2 and Thomas W. Okita

Institute of Biological Chemistry and Graduate Program in Plant Physiology, Washington State University, Pullman, Washington 99164-6340

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.

2 Undergraduate Honors Program.

1 Supported in part by United States Department of Agriculture Grant 82-CRSR-2-1016. Scientific Paper No. 7010, Project 0590, College of Agriculture Research Center, Washington State University, Pullman, WA 99164.




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S. J. Carlson and P. S. Chourey
A Re-Evaluation of the Relative Roles of Two Invertases, INCW2 and IVR1, in Developing Maize Kernels and Other Tissues
Plant Physiology, November 1, 1999; 121(3): 1025 - 1035.
[Abstract] [Full Text]


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Copyright © 1985 by the American Society of Plant Biologists