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-vitroauxin binding to particulate cell fractions from corn coleoptiles
β Scribed by R. Hertel; K. -St. Thomson; V. E. A. Russo
- Publisher
- Springer-Verlag
- Year
- 1972
- Tongue
- English
- Weight
- 788 KB
- Volume
- 107
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
When low concentrations (e.g. 10(-6) M) of labelled 3-indoleacetic acid ((14)C-IAA) or Ξ±-naphthaleneacetic acid ((14)C-NAA) are added in vitro to homogenates of corn coleoptiles, radioactivity is reversibly bound to pelletable particles. From the saturation kinetics of the binding it is possible to estimate an apparent K M between 10(-6) M and 10(-5) M and a concentration of specific sites of 10(-7)-10(-6) M per tissue volume.The binding is auxin-specific. Among many compounds tested, only auxins and such auxin analogues that are known to interact directly with auxin in transport and/or growth were found to interfere with this binding. For instance, the growth-active D-dichlorophenoxyisopropionic acid at 10(-4) M inhibits (14)C-NAA binding more than the less active L-isomer.The auxin-binding fractions are practically free of DNA and cytochrome-C oxidase and contain binding sites for 1-naphthylphthalamic acid. The results are discussed in context with the hyothesis-derived mainly from physiological data-that auxin receptors are localized at the plasma membrane.
π SIMILAR VOLUMES
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
A binding site for auxins was found in the 50,000g pellet from a homogenate of shoots from dark-grown wheat seedlings. The optimum conditions for the binding of native auxin, IAA, were within the range of physiological conditions of growth (pH 5.2, temperature 20Β°C). The binding site displayed a hig