Primary translation products, biosynthesis, and tissue specificity of the major surfactant protein in rat

Joanna Floros, David Phelps, S. Kourembanas, H. W. Taeusch

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Rat lung tissue was labeled with [35S]methionine and the major surfactant-associated proteins immunoprecipitated using a specific antiserum. The protein pattern obtained was very similar to that seen in rat bronchoalveolar lavage. Rat lung mRNA was subsequently translated in an in vitro rabbit reticulocyte system, and surfactant-associated protein-related polypeptides were immunoprecipitated. A 26-kDa polypeptide was identified and characterized as follows. (a) Unlabeled surfactant proteins added to the immunoprecipitation mixture completely inhibited its immunoprecipitation. (b) Two-dimensional gel electrophoresis of the 26-kDa protein resolved it into 3 isoforms. (c) Inclusion of dog pancreatic microsomes in the translation mixture resulted in the formation of two distinct higher molecular weight groups of isoforms, suggesting that the 25-kDa protein is destined to become a glycoprotein. Immunoprecipitation of [35S] methionine-labeled rat lung tissue proteins after tunicamycin treatment resulted in 3 isoforms, identical to the ones seen in the primary translation products. In addition, expression of the surfactant proteins appears specific to the lung.

Original languageEnglish (US)
Pages (from-to)828-831
Number of pages4
JournalJournal of Biological Chemistry
Volume261
Issue number2
StatePublished - Jan 1 1986

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Organ Specificity
Biosynthesis
Surface-Active Agents
Rats
Tissue
Proteins
Immunoprecipitation
Lung
Protein Isoforms
Methionine
Tunicamycin
Peptides
Reticulocytes
Electrophoresis, Gel, Two-Dimensional
Bronchoalveolar Lavage
Microsomes
Electrophoresis
Immune Sera
Glycoproteins
Molecular Weight

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "Rat lung tissue was labeled with [35S]methionine and the major surfactant-associated proteins immunoprecipitated using a specific antiserum. The protein pattern obtained was very similar to that seen in rat bronchoalveolar lavage. Rat lung mRNA was subsequently translated in an in vitro rabbit reticulocyte system, and surfactant-associated protein-related polypeptides were immunoprecipitated. A 26-kDa polypeptide was identified and characterized as follows. (a) Unlabeled surfactant proteins added to the immunoprecipitation mixture completely inhibited its immunoprecipitation. (b) Two-dimensional gel electrophoresis of the 26-kDa protein resolved it into 3 isoforms. (c) Inclusion of dog pancreatic microsomes in the translation mixture resulted in the formation of two distinct higher molecular weight groups of isoforms, suggesting that the 25-kDa protein is destined to become a glycoprotein. Immunoprecipitation of [35S] methionine-labeled rat lung tissue proteins after tunicamycin treatment resulted in 3 isoforms, identical to the ones seen in the primary translation products. In addition, expression of the surfactant proteins appears specific to the lung.",
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Primary translation products, biosynthesis, and tissue specificity of the major surfactant protein in rat. / Floros, Joanna; Phelps, David; Kourembanas, S.; Taeusch, H. W.

In: Journal of Biological Chemistry, Vol. 261, No. 2, 01.01.1986, p. 828-831.

Research output: Contribution to journalArticle

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