Mathematics – Logic
Scientific paper
Mar 1977
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1977natur.266..268v&link_type=abstract
Nature, Volume 266, Issue 5599, pp. 268-269 (1977).
Mathematics
Logic
1
Scientific paper
THE demonstration by Hertel et al.1 of reversible, high-affinity binding of auxins to membranous preparations from corn coleoptiles provided for the first time a reliable and readily accessible system for the study of potential receptor-phytohormone interactions. In a detailed investigation of the binding kinetics and specificity of this system, we presented evidence for the presence of two classes of auxin-binding sites with differing affinities and specificities2,3. Site 1, with a KD for the synthetic auxin 1-naphthalene-acetic acid (NAA) of 0.14 µM, was able to bind both auxins and physiologically inactive analogues, whereas site (KD for NAA = 1.7 µM) displayed binding specificity compatible with that expected of an auxin receptor2 and was located in a heavier membrane population, enriched in plasma membrane3. Auxin-binding activity can be readily solubilised from the membranes with Triton X-100 (ref. 2), but our attempts to purify such extracts further have met with only limited success. I report here that both binding sites can be conveniently removed from the membranes without detergent and purified approximately 100-fold in two steps.
No associations
LandOfFree
Solubilisation and partial purification of auxin-binding sites of corn membranes does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Solubilisation and partial purification of auxin-binding sites of corn membranes, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Solubilisation and partial purification of auxin-binding sites of corn membranes will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-1849582