Yeagle P L, Romans A Y
Biophys J. 1981 Feb;33(2):243-52. doi: 10.1016/S0006-3495(81)84885-0.
Glycophorin, the MN glycoprotein from the erythrocyte membrane, was recombined with egg phosphatidylcholine and with the total lipid extract from human erythrocyte membranes in a membranous form. 31P-nuclear magnetic resonance (NMR) spectra of the recombinants resembled spectra obtained from unsonicated phospholipid dispersions and biological membranes. The glycophorin/phospholipid ratio in these recombinants was varied from approximately 50:1 (lipid/protein) to 200:1, and 31P-NMR spectral intensities were obtained. Comparison of these intensities to that expected based on a pure phospholipid standard revealed that there were two phospholipid environments in the recombinants: one immobilized by the protein, and one slightly disordered and nonimmobilized. A relatively constant number of phospholipids were immobilized per glycophorin at all lipid/protein ratios studied.
血型糖蛋白，即来自红细胞膜的MN糖蛋白，与卵磷脂以及人红细胞膜的总脂质提取物以膜状形式进行了重组。重组体的31P-核磁共振（NMR）谱类似于从未经超声处理的磷脂分散体和生物膜获得的谱。这些重组体中的血型糖蛋白/磷脂比率从大约50:1（脂质/蛋白质）变化到200:1，并获得了31P-NMR谱强度。将这些强度与基于纯磷脂标准预期的强度进行比较，结果表明重组体中有两种磷脂环境：一种被蛋白质固定，另一种略有无序且未被固定。在所研究的所有脂质/蛋白质比率下，每个血型糖蛋白固定的磷脂数量相对恒定。
