Biosynthesis and in vitro translation of the major surfactant-associated protein from human lung

Joanna Floros, David Phelps, H. W. Taeusch

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Abstract

We have characterized a 32,000-36,000-dalton sialoglycoprotein group that is an integral component of the lipoprotein complex called pulmonary surfactant. Our results from the cell-free translation of human lung RNA show that this protein consists of two similarly-sized precursor components of about 29,000-31,000 daltons. Tunicamycin treatment of the lung tissue prevents formation of the normal protein and results in the accumulation of these precursor components which are also seen under normal conditions in very small amounts. Although in vitro translation in the presence of dog pancreatic microsomes suggests that a cleavable signal peptide sequence is present in these precursor molecules, it does not appear that this cleavage occurs in vivo.

Original languageEnglish (US)
Pages (from-to)495-500
Number of pages6
JournalJournal of Biological Chemistry
Volume260
Issue number1
StatePublished - Jan 1 1985

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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