Abstract
Several years ago we described (Fox and Erion, 1975, 1977) the properties of a soluble protein (CBF-1) isolated from wheat germ which binds eytokinins with relatively high affinity and specificity. This study was stimulated by an earlier report from investigators in Letham’s laboratory (Berridge et al., 1970) who described nonsaturable, multisite, reversible binding of kinetin to ribosomes isolated from Brassica pekinensis leaves. Although Scatchard plots of binding were not presented and the investigators were unable to solubilize a binding substance, their data indicate a low affinity, nonspecific binding of the kind seen in wheat germ ribosomes (Fox and Erion, 1977) at the high cytokinin concentrations used in their study. However a wheat embryo protein having a relatively high affinity for eytokinins has recently been studied in two other laboratories (Polya and Davis, 1978; Polya and Bowman, 1979; Moore, 1979) and is apparently identical with CBF-1.
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Abbreviations
- CBF-1:
-
wheat germ cytokinin binding protein
- bzl6 Ade:
-
6-benzylaminopurine
- i6 Ade:
-
6(Δ2-isopentenylamino) purine
- io6 Ade:
-
Zeatin
- OH-PA:
-
6 (5’-hydroxy-n-pentylamino) purine
- i6 Ado:
-
N6 (Δ2-isopentenyl)adenosine
- io6 Ado:
-
Zeatin Riboside
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© 1981 Springer-Verlag, Berlin Heidelberg
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Keim, P., Erion, J., Fox, J.E. (1981). The Current Status of Cytokinin-Binding Moieties. In: Guern, J., Péaud-Lenoël, C. (eds) Metabolism and Molecular Activities of Cytokinins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68035-9_17
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DOI: https://doi.org/10.1007/978-3-642-68035-9_17
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