Identification, isolation, and partial characterization of a 7.5-kDa surfactant-associated protein

Exp Lung Res. 1991 May-Jun;17(3):559-67. doi: 10.3109/01902149109062865.

Abstract

Human surfactant was analyzed for proteins associated with the lipids. Surfactant was isolated from lung lavage by the salt gradient centrifugation method, and the soluble proteins binding to the lipids were recovered by extraction with a low pH buffer. Antiserum to this preparation reacted with surfactant apoprotein A and a 7.5-kDa protein. The 7.5-kDa protein was isolated from reduced and alkylated lung lavage pellet by chromatography. The N-terminal amino acid sequence of the protein indicates that it is a novel protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Centrifugation
  • Humans
  • Immune Sera / immunology
  • Molecular Sequence Data
  • Molecular Weight
  • Proteolipids / chemistry
  • Proteolipids / immunology
  • Proteolipids / isolation & purification*
  • Pulmonary Surfactant-Associated Proteins
  • Pulmonary Surfactants / chemistry
  • Pulmonary Surfactants / immunology
  • Pulmonary Surfactants / isolation & purification*

Substances

  • Amino Acids
  • Immune Sera
  • Proteolipids
  • Pulmonary Surfactant-Associated Proteins
  • Pulmonary Surfactants