Postle A D, Hunt A N, Normand I C
Biochim Biophys Acta. 1985 Dec 4;837(3):305-13. doi: 10.1016/0005-2760(85)90054-2.
Human pulmonary surfactant was purified from bronchoalveolar lavage of patients. The proteins present in surfactant were analyzed by SDS-polyacrylamide gel electrophoresis into serum and non-serum components. One non-serum surfactant protein (Mr = 43 000) was then identified in the 100 000 X g supernatant of a lung homogenate on the basis of phospholipid binding. This lung protein was purified and partially characterized. The presence of 3-methyl histidine and reaction in Western blot analysis with antibody against chicken muscle actin both strongly suggested that the 43 000 Da protein of human surfactant is indeed cytoplasmic actin. It is proposed that this surfactant protein is involved in the secretion and not necessarily in the function of surfactant.
人肺表面活性物质从患者的支气管肺泡灌洗物中纯化得到。通过SDS-聚丙烯酰胺凝胶电泳分析表面活性物质中存在的蛋白质，将其分为血清和非血清成分。然后，基于磷脂结合，在肺匀浆的100000×g上清液中鉴定出一种非血清表面活性蛋白（Mr = 43000）。对这种肺蛋白进行了纯化并部分表征。3-甲基组氨酸的存在以及在蛋白质印迹分析中与抗鸡肌肉肌动蛋白抗体的反应均强烈表明，人表面活性物质的43000 Da蛋白确实是细胞质肌动蛋白。有人提出，这种表面活性蛋白参与表面活性物质的分泌，而不一定参与其功能。
