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

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

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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 - Dec 1 1986

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Floros, J., Steinbrink, R., Jacobs, K., Phelps, D., Kriz, R., Recny, M., Sultzman, L., Jones, S., Taeusch, H. W., & Frank, H. A. (1986). Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein. Journal of Biological Chemistry, 261(19), 9029-9033.