Canine hydrophobic surfactant polypeptide SP-C. A lipopeptide with one thioester-linked palmitoyl group.
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.
Johansson
J
J
Department of Clinical Chemistry, Karolinska Institute, Danderyd Hospital, Sweden.
Persson
P
P
Löwenadler
B
B
Robertson
B
B
Jörnvall
H
H
Curstedt
T
T
D000595:Amino Acid Sequence; D000818:Animals; D004285:Dogs; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010169:Palmitic Acids / Q000032:analysis*; D011510:Proteolipids / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D011663:Pulmonary Surfactants / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D010169:Palmitic Acids; D011510:Proteolipids; D011663:Pulmonary Surfactants