ARTIFICIAL PULMONARY SURFACTANT INHIBITED BY PROTEINS
ARTIFICIAL PULMONARY SURFACTANT INHIBITED BY PROTEINS
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DOI：
10.1152/jappl.1987.62.2.429
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发表时间：
1987-02-01
影响因子：
3.3
通讯作者：
ENHORNING, G
中科院分区：
文献类型：
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作者：
FUCHIMUKAI, T;FUJIWARA, T;ENHORNING, G
用脉动气泡表面活性计，我们评估了各种试剂、纤维蛋白原、人血清、白蛋白和55，000-道尔顿血清蛋白干扰表面活性剂TA的表面活性的能力。从4 mg/ml的最高最终蛋白质浓度开始，将潜在抑制剂分六步稀释至0.125 mg/ml，并将每种浓度与两种最终磷脂浓度（6.25和1.25 mg/ml）的表面活性剂制剂一起进行评价。纤维蛋白原的抑制作用最强，其次是人血清和55，000-道尔顿血清蛋白;最弱的抑制剂是白蛋白。当胆红素以1.73 mg/100 ml溶于人血清的量加入时，其抑制作用显著增强（P < 0.001）。吸附速率，如在产生气泡后2和10秒的表面张力的平均值中所反映的，不脉动，受到浓度超过1 mg/ml的每种含蛋白质的抑制剂的严重影响。当脉动气泡处于最大和最小尺寸时，表面张力显著升高。该效应具有剂量依赖性。在最大尺寸下，在10分钟记录期间没有消失的趋势，但在最小气泡尺寸下，抑制逐渐减弱。我们得出结论，存在于气道中的蛋白质可能严重干扰表面活性剂TA的活性。
With a pulsating bubble surfactometer we assessed the ability of various agents, fibrinogen, human serum, albumin, and a 55,000-dalton serum protein, to interfere with the surface activity of Surfactant TA. From a highest final protein concentration of 4 mg/ml the potential inhibitors were diluted down to 0.125 mg/ml in six steps, and each concentration was evaluated together with two final phospholipid concentrations, 6.25 and 1.25 mg/ml, of the surfactant preparation. The strongest inhibition action was exerted by fibrinogen, followed by human serum and the 55,000-dalton serum protein; the weakest inhibitor was albumin. Bilirubin, when added in an amount of 1.73 mg/100 ml dissolved in human serum, significantly (P < 0.001) augmented the inhibition over that exerted by human serum alone. Adsorption rate, as reflected in the mean value of surface tension 2 and 10 s after creation of a bubble, not pulsating, was seriously affected by each of the protein-containing inhibitors in concentrations exceeding 1 mg/ml. Surface tension was raised significantly when the pulsating bubble was at maximal and minimal size. The effect was dose dependent. At maximal size it showed no tendency to disappear during the 10-min recording, but at minimal bubble size the inhibition gradually diminished. We conclude that protein present in the airways may seriously interfere with the activity of Surfactant TA.