A Cytokinin-binding Protein from Wheat Germ
Author(s) -
F. Hardy Moore
Publication year - 1979
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.64.4.594
Subject(s) - sephadex , ammonium sulfate precipitation , kinetin , cytokinin , chemistry , dissociation constant , chromatography , biochemistry , affinity chromatography , zeatin , stereochemistry , size exclusion chromatography , auxin , enzyme , receptor , explant culture , in vitro , gene
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; N(6)-benzylaminopurine and N(6)-(Delta(2)-isopentenyl)adenine were also strongly bound. Little affinity was exhibited toward either cis-zeatin or trans-zeatin.
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