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. 1979 Oct;64(4):594–599. doi: 10.1104/pp.64.4.594

A Cytokinin-binding Protein from Wheat Germ

Isolation by Affinity Chromatography and Properties 1,2

F Hardy Moore III a,3
PMCID: PMC543144  PMID: 16661016

Abstract

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-(Δ2-isopentenyl)adenine were also strongly bound. Little affinity was exhibited toward either cis-zeatin or trans-zeatin.

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Selected References

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