Phelps D S, Smith L M, Taeusch H W
Am Rev Respir Dis. 1987 May;135(5):1112-7. doi: 10.1164/arrd.1987.135.5.1112.
Chloroform:methanol (2:1) extracts of bovine surfactant were subjected to LH-20 Sephadex chromatography in order to isolate a 6,000-dalton surfactant protein. The 6,000-dalton protein eluted in the void volume and was shown to be homogeneous by protein sequencing, although SDS gel electrophoresis revealed bands of 6, 14, and 18 kDa. The N-terminal sequence obtained was very hydrophobic, as was the amino acid composition of the 6,000-dalton protein. An antiserum raised against the low molecular weight protein fraction from TA surfactant recognized the 6,000-dalton bovine and human proteins in addition to protein bands at 14,000 and 18,000 daltons. These bands appear to be aggregates of the 6,000-dalton protein. No cross-reactivity of the 6,000-dalton protein antiserum could be demonstrated with the 35,000-dalton surfactant-associated protein. These studies strongly suggest that the 35,000- and 6,000-dalton surfactant proteins do not have a precursor-product relationship.
为了分离出一种6000道尔顿的表面活性剂蛋白，对牛表面活性剂的氯仿：甲醇（2:1）提取物进行了LH - 20葡聚糖凝胶色谱分析。6000道尔顿的蛋白在空体积中洗脱出来，通过蛋白质测序显示其为均一的，尽管SDS凝胶电泳显示出6、14和18千道尔顿的条带。所获得的N端序列以及6000道尔顿蛋白的氨基酸组成都具有很强的疏水性。一种针对来自TA表面活性剂的低分子量蛋白组分产生的抗血清，除了识别14000和18000道尔顿的蛋白条带外，还识别6000道尔顿的牛和人蛋白。这些条带似乎是6000道尔顿蛋白的聚集体。未证明6000道尔顿蛋白抗血清与35000道尔顿的表面活性剂相关蛋白有交叉反应。这些研究强烈表明，35000道尔顿和6000道尔顿的表面活性剂蛋白不存在前体 - 产物关系。
