Hormonal Regulation Colloquium, London
نویسندگان
چکیده
demonstrate that the light band has the kinetic properties of site 1 with respect to naphth-1-ylacetate binding, whereas the heavy band is kinetically equivalent to site 2. Further, the specificities of the resolved sites towards other auxins and analogues are identical with those deduced from experiments with unfractionated membrane preparations. In summary, membranous preparations from maize coleoptiles contain two sets of high-affinity auxin-binding sites, which may be resolved by discontinuous-sucrosegradient centrifugation. The lower-affinity site (site 2) is specific for compounds with auxin activity, is located in fractions enriched in plasma membrane and may represent an auxin-receptor site. The possible physiological function of the apparently non-specific site (site 1) remains unknown at present.
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