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.
Shanghai Institute of Physiology, Chinese Academy of Sciences, People's Republic of China.
G P
GP
Zhang
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Shi
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Wang
W Y
WY
Liu
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