Characterization and partial amino acid sequence of a low molecular weight surfactant protein

David Phelps, L. M. Smith, H. W. Taeusch

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)1112-1117
Number of pages6
JournalAmerican Review of Respiratory Disease
Volume135
Issue number5
Publication statusPublished - Dec 1 1987

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All Science Journal Classification (ASJC) codes

  • Pulmonary and Respiratory Medicine

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