Cation channel formed at lipid bilayer by Cinnamomin, a new type II ribosome-inactivating protein.
Cinnamomin, a new type II ribosome-inactivating protein, purified from the seeds of Cinnamonum camphora is reconstituted into the membranes of planar lipid bilayer and giant liposome. The channel-forming activity of the cinnamomin is found and cation permeability of the channel is characterized by patch clamp. In an asymmetric solution system, bath 150/pipette 100 mM KCl, the unit conductance is 140+/-7 pS and the reversal potential is 10.4+/-0.6 mV, very close to the theoretical value of the K+ electrode. The results offer an interpretation for internalization of the RIP and the cytotoxicity difference between single and two chain RIP.
Zhang
G P
GP
Shanghai Institute of Physiology, Chinese Academy of Sciences, People's Republic of China.
Shi
Y L
YL
Wang
W P
WP
Liu
W Y
WY
D020418:Algal Proteins; D007473:Ion Channels / Q000378:metabolism*; D019770:Lauraceae / Q000737:chemistry; D008051:Lipid Bilayers / Q000378:metabolism*; D018408:Patch-Clamp Techniques; D011188:Potassium / Q000378:metabolism; D011506:Proteins / Q000494:pharmacology*; D054790:Ribosome Inactivating Proteins, Type 2; D012270:Ribosomes / Q000187:drug effects*; D012964:Sodium / Q000378:metabolism
D020418:Algal Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D011506:Proteins; D054790:Ribosome Inactivating Proteins, Type 2; C061930:cinnamomin, Phytophthora cinnamomi; D012964:Sodium; D011188:Potassium