Kersh G J, Tomich J M, Montal M
Department of Biology, University of California, San Diego, La Jolla 92093-0319.
Biochem Biophys Res Commun. 1989 Jul 14;162(1):352-6. doi: 10.1016/0006-291x(89)92003-2.
A synthetic peptide with the sequence of the M2 delta segment of the nicotinic acetylcholine receptor from Torpedo californica forms pores in human erythrocyte membranes as determined by hemoglobin and potassium release. This peptide forms a permeability pathway with an apparent cross-sectional diameter of 7-9 A. The M2 delta pore is oligomeric and a pentamer is the species that accounts for the properties of the permeation path. Peptides that mimic other identifiable segments of the Torpedo acetylcholine receptor, M1 delta and MIR, do not form channels in erythrocytes under the same conditions.
通过血红蛋白和钾离子释放测定，来自加州电鳐的烟碱型乙酰胆碱受体M2δ片段序列的合成肽可在人红细胞膜上形成孔道。该肽形成了一个表观横截面直径为7 - 9埃的通透性通道。M2δ孔道是寡聚体，五聚体是解释渗透路径特性的物种。在相同条件下，模拟加州电鳐乙酰胆碱受体其他可识别片段（M1δ和MIR）的肽不会在红细胞中形成通道。
