Solubilisation and partial purification of a fusicoccin-receptor complex from maize microsomes

摘要: Abstract Fusicoccin (FC) specifically bound to microsomal preparations from maize coleoptiles can be partially solubilised by treatments with Triton X-100, deoxycholate (DOC), SDS, urea, sodium perchlorate and trypsin. In the cases of deoxycholate, percholate or trypsin a consistent fraction FC appears still macromolecular component. On Sephadex G-200 filtration perchlorate-solubilised FC-macromolecule complex shows well-defined peak, corresponding molecular weight approx. 80 000. Acrylamide disc gel electrophoresis FC-containing fractions chromatography seperates in single, narrow peak minor protein peak. These data are interpreted as suggesting that high-affinity, low-reversibility is due interaction between single receptor protein, localised at plasmamembrane, possibly involved physiological activity toxin.