Takahashi A, Fujiwara T
Biochem Biophys Res Commun. 1986 Mar 13;135(2):527-32. doi: 10.1016/0006-291x(86)90026-4.
The chemical and biophysical properties of the proteins in the lipid extracts of lung surfactant have not clearly been determined. These proteins were isolated from lung surfactant lipids by Sephadex LH-20 chromatography and purified with silicic acid chromatography followed by dialysis against organic solvents. The proteolipid thus obtained had a protein to phospholipid ratio of 3 to 1 (w/w). The proteolipid apoprotein had a nominal molecular weight of ca. 5 kDa. We evaluated the functional role of this proteolipid by combining it with proteolipid-depleted surfactant lipids or synthetic dipalmitoylphosphatidylcholine (DPPC) and then measuring with a pulsating bubble surfactometer. The proteolipid and DPPC recombinant reproduced the surface activity of natural lung surfactant. We conclude that this 5 kDa proteolipid apoprotein is a functionally important constituent of lung surfactant.
肺表面活性剂脂质提取物中蛋白质的化学和生物物理特性尚未明确确定。这些蛋白质通过葡聚糖LH - 20色谱法从肺表面活性剂脂质中分离出来，并用硅酸色谱法纯化，然后用有机溶剂进行透析。由此获得的蛋白脂质的蛋白质与磷脂之比为3比1（w/w）。该蛋白脂质载脂蛋白的标称分子量约为5 kDa。我们通过将这种蛋白脂质与去除蛋白脂质的表面活性剂脂质或合成二棕榈酰磷脂酰胆碱（DPPC）结合，然后用脉动气泡表面张力仪进行测量，来评估该蛋白脂质的功能作用。蛋白脂质和DPPC重组体重现了天然肺表面活性剂的表面活性。我们得出结论，这种5 kDa的蛋白脂质载脂蛋白是肺表面活性剂功能上重要的组成部分。
