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. 1979 Sep;64(3):387–392. doi: 10.1104/pp.64.3.387

Ligand Specificity of a High Affinity Cytokinin-binding Protein 1

Gideon M Polya a, Janette A Bowman a
PMCID: PMC543097  PMID: 16660972

Abstract

A soluble cytokinin-binding protein from wheat germ that has a high affinity for a range of purine cytokinins also interacts with a variety of nonpurine compounds that can affect cytokinin-modified processes in animal or plant cells or which bind to proteins known to interact with certain cytokinins. A variety of structurally disparate compounds which inhibit chloroplast photosystem II activity (including phenylurea, carbanilate, and alkylamino-2-chloro-sym-triazine compounds) displace kinetin from the protein in an apparently competitive fashion. However, various energy transfer inhibitors (including organotin compounds and N,N′-dicy-clohexylcarbodiimide) also inhibit kinetin binding to the protein. N6,2-0′-Dibutyryl-3′,5′-cyclic AMP and 1-methyl-3-isobutylxanthine (the effects of which on fibroblast morphology and motility can be mimicked by cytokinins) are inhibitors of kinetin binding to the protein. A variety of compounds that can have antimitotic effects (including 1-methyl-3-isobutylxanthine and certain alkylated cyclic nucleotide, carbanilate, and tryptamine compounds) displace kinetin from the protein. However, a variety of indole derivatives also displace kinetin from the cytokinin-binding protein, which in a qualitative sense has a broad ligand specificity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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