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Plant Physiology 64:594-599 (1979)
© 1979 American Society of Plant Biologists

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Articles

A Cytokinin-binding Protein from Wheat Germ

Isolation by Affinity Chromatography and Properties 1,2

F. Hardy Moore, III3

a Department of Botany, University of Wisconsin, Madison, Wisconsin 53706

A cytokinin-binding protein has been isolated from wheat germ via ammonium sulfate precipitation, carboxymethyl Sephadex chromatography, and affinity chromatography on a column substituted with a derivative of kinetin riboside. On Sephadex G-200, the protein migrated with an apparent molecular weight of 122,000 daltons. The dissociation constant for kinetin was determined by equilibrium dialysis to be 1.2 micromolar; N6-benzylaminopurine and N6-({Delta}2-isopentenyl)adenine were also strongly bound. Little affinity was exhibited toward either cis-zeatin or trans-zeatin.

3 Present address: Roger Adams Laboratory, School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801.

1 This work was supported by National Science Foundation Grant BMS-72-02226 to Professor Folke Skoog and by research funds granted to the Institute of Plant Development by the University of Wisconsin-Madison Graduate School.

2 The work described herein was submitted in partial fulfillment of the requirements for the Ph.D. degree in the Department of Botany, University of Wisconsin-Madison.






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Copyright © 1979 by the American Society of Plant Biologists