Isolation and characterization of a cytokinin-binding protein from etiolated maize seedlings

F. A. Brovko, T. K. Zagranichnaya, Kh M. Boziev, V. M. Lipkin, N. N. Karavaiko, S. Yu Selivankina, O. N. Kulaeva

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8 Scopus citations


A cytokinin-binding protein (CBP) was isolated from etiolated maize (Zea mays L.) seedlings by two protocols. Ammonium sulfate fractionation, hydrophobic chromatography on Toyopearl HW-60, and affinity chromatography on immobilized trans-zeatin were used for CBP isolation according to the first protocol. The second protocol included a combination of ion-exchange chromatography and gel filtration followed by affinity chromatography on zeatin riboside-Toyopearl as in the first protocol. In order to remove proteins that could be nonspecifically bound to the affinity matrix, chromatography on adenosine-Toyopearl preceded chromatography on zeatin riboside-Toyopearl. Following these procedures, a CBP with a molecular weight of 70 kD was isolated. This protein specifically and reversibly bound dihydrozeatin and, in the presence of trans-zeatin, activated in vitro RNA synthesis in a system containing chromatin-bound RNA polymerase I from barley leaves. The protein cross-reacted with anti-idiotypic antibodies isolated from antizeatin serum, and, therefore, these antibodies could be considered antibodies to zeatin-binding protein. The data thus obtained indicate that the isolated CBP is a cytokinin receptor.

Original languageEnglish
Pages (from-to)467-473
Number of pages7
JournalRussian Journal of Plant Physiology
Issue number4
StatePublished - Jul 1996


  • Cytokinin-binding proteins
  • Cytokinins
  • Transcription activation
  • Zea mays

ASJC Scopus subject areas

  • Plant Science


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