ISSN:
1432-2048
Keywords:
Cytokinin binding
;
Glycoprotein
;
Triticum
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract A soluble protein that interacts with a range of cytokinins was extensively purified from wheat (Triticum aestivum L.) germ. This protein has a K d for kinetin of 2×10-7 M. The binding of kinetin to the protein is inhibited by low concentrations of synthetic and naturally-occurring cytokinins including N6-benzyladenine, N6-benzyladenosine, kinetin riboside, N6-dimethylallyladenine, N6-dimethylallyladenosine, zeatin, zeatin riboside, N6-dimethyladenine and N6-dimethyladenosine. Adenine, adenosine and several non-N6-substituted adenine derivatives were ineffective as inhibitors of kinetin binding. While N6-butyryl-3′,5′-cyclic AMP, N6,2-O′-dibutyryl-3′,5′-cyclic AMP and 2′,3′-cyclic AMP inhibited binding of kinetin to the protein, 3′,5′-cyclic AMP was ineffective. The kinetin-binding protein is heat-labile and pronase-sensitive. Kinetin-binding activity exactly co-chromatographs with a single peak of carbohydrate and protein on gel-filtration and is displaced from concanavalin A-Sepharose 4B by α-methylglucoside. On gel filtration, the kinetin-binding protein behaves as a soluble protein with an apparent molecular weight of 180,000 daltons.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00387139
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