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Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein

  • J. Floros
  • , R. Steinbrink
  • , K. Jacobs
  • , D. Phelps
  • , R. Kriz
  • , M. Recny
  • , L. Sultzman
  • , S. Jones
  • , H. W. Taeusch
  • , H. A. Frank

Research output: Contribution to journalArticlepeer-review

Abstract

A group of 35,000-dalton sialoglycoproteins is the major non-serum protein component of pulmonary surfactant. Tryptic fragments of these proteins were sequenced, and oligonucleotide probes were synthesized based on the amino acid sequences. A human lung cDNA library was then screened using the oligonucleotide probes, and clones coding for these proteins were identified and characterized. By in vitro transcription-translation experiments we have associated individual clones with particular proteins. The data suggest that co-translational modifications of two primary translation products account for many of the isoforms observed by two-dimensional gel electrophoresis in the precursors of 35,000-dalton sialoglycoproteins.

Original languageEnglish (US)
Pages (from-to)9029-9033
Number of pages5
JournalJournal of Biological Chemistry
Volume261
Issue number19
StatePublished - 1986

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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