Canine hydrophobic surfactant polypeptide SP-C. A lipopeptide with one thioester-linked palmitoyl group

FEBS Lett. 1991 Apr 9;281(1-2):119-22. doi: 10.1016/0014-5793(91)80373-b.

Abstract

The amino acid sequence and the posttranslational modification of the hydrophobic surfactant polypeptide SP-C from canine, rabbit and bovine lungs were established by direct sequence analysis and plasma-desorption time-of-flight mass spectrometry. The results reveal that canine SP-C has only one cysteine residue which, however, is palmitoylated, like the two Cys residues in other characterized SP-C molecules. In addition, canine SP-C is N-terminally truncated, with only 34 amino acid residues in its longest form. Thus, SP-C molecules can apparently vary to some extent in the N-terminal lipid-modified part, whereas the extremely hydrophobic middle and C-terminal parts are well conserved.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Dogs
  • Humans
  • Mass Spectrometry
  • Molecular Sequence Data
  • Molecular Weight
  • Palmitic Acids / analysis*
  • Proteolipids / chemistry
  • Proteolipids / genetics*
  • Proteolipids / isolation & purification
  • Pulmonary Surfactants / chemistry
  • Pulmonary Surfactants / genetics*
  • Pulmonary Surfactants / isolation & purification
  • Sequence Homology, Nucleic Acid

Substances

  • Palmitic Acids
  • Proteolipids
  • Pulmonary Surfactants