Lung 'surfactant convertase' is a member of the carboxylesterase family

S. Krishnasamy, N. J. Gross, A. L. Teng, R. M. Schultz, Rajiv Dhand

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The extracellular conversion of lung surfactant from tubular myelin to the small vesicular form has previously been shown to require a serine-active enzyme called 'surfactant convertase.' In the present study, a 72 kD serine-active enzyme previously identified in mouse lung alveolar lavage and having convertase activity was partially sequenced. Sixty-eight residues obtained from amino acid sequencing of this protein show that it is a new member of the mouse carboxylesterase family (EC 3.1.1.1). The 72 kD lung protein also has esterase activity. A commercial esterase of the same family was able to reproduce surfactant convertase bioactivity in vitro, unlike several serine proteinases previously tested. We conclude that surfactant convertase is a carboxylesterase which mediates a biochemical step in the extracellular metabolism of surfactant.

Original languageEnglish (US)
Pages (from-to)180-184
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume235
Issue number1
DOIs
StatePublished - Jun 9 1997
Externally publishedYes

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Carboxylesterase
Surface-Active Agents
Lung
Esterases
Serine
Protein Sequence Analysis
Serine Proteases
Bronchoalveolar Lavage
Enzymes
Bioactivity
Metabolism
Proteins
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Lung 'surfactant convertase' is a member of the carboxylesterase family. / Krishnasamy, S.; Gross, N. J.; Teng, A. L.; Schultz, R. M.; Dhand, Rajiv.

In: Biochemical and Biophysical Research Communications, Vol. 235, No. 1, 09.06.1997, p. 180-184.

Research output: Contribution to journalArticle

Krishnasamy, S. ; Gross, N. J. ; Teng, A. L. ; Schultz, R. M. ; Dhand, Rajiv. / Lung 'surfactant convertase' is a member of the carboxylesterase family. In: Biochemical and Biophysical Research Communications. 1997 ; Vol. 235, No. 1. pp. 180-184.
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