Suzuki Y
J Lipid Res. 1982 Jan;23(1):62-9.
Lipid-protein complexes reconstituted from pig surfactant lipids and proteins were investigated for surface adsorption, minimum surface tension, stability index, and surface compressibility. Lipid constituents remained unchanged with procedures for the reconstitution. An apoprotein with a nominal molecular weight of 15,000 daltons significantly accelerated the lipid-protein complex to absorb the air-water interface. A 34,000-dalton apoprotein slightly modified the surface adsorption and the surface activity when it was incorporated into the lipid-protein complex formed from lipids and 15,000-dalton apoprotein. No significant surface adsorption was found in lipid vesicles even with the same lipid constituents as in the lipid-protein complex. In the lipid-protein complex prepared by changing the content of cholesterol and phosphatidylglycerol, cholesterol affected both the minimum surface tension and the surface compressibility while phosphatidylglycerol had little effect on the surface activity of the complex.
对由猪表面活性剂脂质和蛋白质重构而成的脂蛋白复合物进行了表面吸附、最低表面张力、稳定性指数和表面压缩性的研究。脂质成分在重构过程中保持不变。一种标称分子量为15,000道尔顿的载脂蛋白显著加速了脂蛋白复合物对空气-水界面的吸附。一种34,000道尔顿的载脂蛋白在掺入由脂质和15,000道尔顿载脂蛋白形成的脂蛋白复合物时，对表面吸附和表面活性有轻微的改变。即使脂质小泡具有与脂蛋白复合物相同的脂质成分，也未发现明显的表面吸附。在通过改变胆固醇和磷脂酰甘油含量制备的脂蛋白复合物中，胆固醇影响最低表面张力和表面压缩性，而磷脂酰甘油对复合物的表面活性影响很小。
