Characterization and partial amino acid sequence of a low molecular weight surfactant protein.
Characterization and partial amino acid sequence of a low molecular weight surfactant protein.
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低分子量表面活性剂蛋白的表征和部分氨基酸序列。
DOI：
10.1164/arrd.1987.135.5.1112
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Taeusch,HW
中科院分区：
文献类型：
--
作者：
Phelps,DS;Smith,LM;Taeusch,HW
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. TheN-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.
