Keough K M, Parsons C S, Tweeddale M G
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
Can J Physiol Pharmacol. 1989 Jun;67(6):663-8. doi: 10.1139/y89-106.
The influence of human albumin, alpha-globulin, and fibrinogen on the actions of porcine pulmonary surfactant in a pulsating bubble surfactometer has been investigated. All three proteins detracted from the ability of the surfactant to adsorb to the air-water interface. The proteins also reduced the ability of surfactant to lower the opening pressures of bubbles cycling between different sizes in suspensions of surfactant. This was equivalent to restricting the ability of the surfactant to achieve low surface tension during compression of the surface. Of the three proteins, globulin competed most effectively with surfactant during the adsorption process, and albumin competed the least effectively. The proteins also may have interfered with the processes of surface refinement, which usually yields a monolayer enriched enough in dipalmitoyl phosphatidylcholine to achieve very low surface tension (very low opening pressures in the bubbles). Of the three proteins tested, albumin was least deleterious to surface refining whereas globulin and fibrinogen appeared to be about equally detrimental to the process.
研究了人白蛋白、α-球蛋白和纤维蛋白原对脉动气泡表面张力仪中猪肺表面活性剂作用的影响。这三种蛋白质均降低了表面活性剂吸附到气-水界面的能力。这些蛋白质还降低了表面活性剂降低表面活性剂悬浮液中不同大小气泡循环时的开启压力的能力。这相当于限制了表面活性剂在表面压缩过程中达到低表面张力的能力。在这三种蛋白质中，球蛋白在吸附过程中与表面活性剂的竞争最有效，而白蛋白的竞争最无效。这些蛋白质还可能干扰了表面细化过程，表面细化通常会产生富含二棕榈酰磷脂酰胆碱的单分子层，从而实现非常低的表面张力（气泡中的开启压力非常低）。在测试的三种蛋白质中，白蛋白对表面细化的损害最小，而球蛋白和纤维蛋白原对该过程的损害似乎大致相同。
