Cytokinin-induced bud formation in moss protonemata is specific for cytokinin bases, their ribosides being relatively inactive. Binding of [3H]benzyladenine (BA) to a 13,000 80,000 x g subcellular fraction from extracts of F u n a r i a h y g r o m e t r i c a (L.) Sibth. was measured by a centrifug
In vitro cytokinin binding to a particulate fraction of tobacco cells
β Scribed by Michael R. Sussman; Hans Kende
- Publisher
- Springer-Verlag
- Year
- 1978
- Tongue
- English
- Weight
- 888 KB
- Volume
- 140
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
At least two types of cytokinin-binding sites are present in a particulate fraction of tobacco (Nicotiana tabacum L.) cells that sediments at 80,000 x g. The major binding component has a low affinity towards cytokinins, is resistant to heating at 100 ~ C, and is not specific for biologically active cytokinin analogues. The second site occurs in much lower frequency, is heat labile, shows high affinity towards cytokinins, and is specific for biologically active analogs of the hormone. The testing for binding specificity was mainly performed with a series of halogenated benzyladenine derivatives having a wide range of biological activities. The low-affinity binding site shows some of the same features as talcum powder, a non-biological material which binds cytokinins in a non-specific fashion. The properties of the high-affinity binding site are consistent with the expected characteristics of a cytokinin receptor. However, the role of the observed high-affinity binding site with regard to the biological action of cytokinins is not yet known.
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