Lea E J, Rich G T, Segrest J P
Biochim Biophys Acta. 1975 Feb 28;382(1):41-50. doi: 10.1016/0005-2736(75)90370-3.
The insoluble peptide, T(is), prepared by trypsin hydrolysis of the MN-glycoprotein (glycophorin) of the human erythrocyte has been incorporated into phospholipid membranes in the form of liposomes and black lipid membranes. The permeability of liposome membranes to 42K+ and of black lipid membranes to water and ions is increased significantly by the presence of the T(is) peptide. Electrophoresis measurements indicate that these effects are not due to the T(is) peptide carrying a net charge. The results suggest that the peptide causes local disordering of the bilayer membrane structures. This is considered in the light of findings published elsewhere: that the MN-glycoprotein penetrates through the cell membrane via a non-polar segment of its polypeptide chain, which is contained intact within the T(is) peptide; that the T(is) peptide is partially helical when associated with phospholipid and forms multimeric 8.0 nm structures within the hydrophobic plane of phospholipid bilayers.
通过胰蛋白酶水解人红细胞的MN糖蛋白（血型糖蛋白）制备的不溶性肽T(is)，已以脂质体和黑色脂质膜的形式掺入磷脂膜中。T(is)肽的存在显著增加了脂质体膜对42K+的通透性以及黑色脂质膜对水和离子的通透性。电泳测量表明，这些效应并非由于T(is)肽带有净电荷。结果表明，该肽导致双层膜结构局部无序。结合其他地方发表的研究结果来考虑这一点：MN糖蛋白通过其多肽链的非极性片段穿透细胞膜，该片段完整地包含在T(is)肽中；T(is)肽与磷脂结合时部分呈螺旋状，并在磷脂双层的疏水平面内形成8.0纳米的多聚体结构。
