Pérez-Gil J, Nag K, Taneva S, Keough K M
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
Biophys J. 1992 Jul;63(1):197-204. doi: 10.1016/S0006-3495(92)81582-5.
The hydrophobic pulmonary surfactant protein SP-C has been isolated from porcine lung surfactant, and it has been incorporated into monolayers of dipalmitoylphosphatidylcholine (DPPC). The monolayers, which contained 1 mol% of a fluorescently-labeled phosphatidylcholine, were observed under various states of compression in an epifluorescence surface balance. SP-C altered the packing arrangements of DPPC in the monolayer, causing the production of many more, smaller condensed lipid domains in its presence than in its absence.
疏水性肺表面活性蛋白SP-C已从猪肺表面活性剂中分离出来,并被整合到二棕榈酰磷脂酰胆碱(DPPC)单层中。这些含有1摩尔%荧光标记磷脂酰胆碱的单层在落射荧光表面天平中于各种压缩状态下进行观察。SP-C改变了单层中DPPC的堆积排列,导致其存在时比不存在时产生更多更小的凝聚脂质域。