Abstract
Several attempts have been made to purify auxin receptors by affinity chromatography, beginning with the use of 2,4-D-lysine coupled to activated Sepharose to Isolate from maize and pea extracts proteins that promoted DNA-dependent RNA synthesis (Venis, 1971). Similar fractions were subsequently isolated from soybean on the same matrix (Rizzo et al., 1977). However, in neither case was activity auxin-dependent, nor could auxin binding be demonstrated. The analogous IAA-lysine adsorbent was reported to Isolate homogeneous auxin-binding protein from coconut endosperm (Roy and Biswas, 1977), but many questions have been raised about this system (Venis, 1985).
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Venis, M.A. (1987). Can Auxin Receptors be Purified by Affinity Chromatography?. In: Klämbt, D. (eds) Plant Hormone Receptors. NATO ASI Series, vol 10. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-72779-5_3
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DOI: https://doi.org/10.1007/978-3-642-72779-5_3
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