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

FEBS Letters

Persson, Per³  Curstedt, Tore¹  Johansson, Jan⁴  Löwenadler, Björn³  Jörnvall, Hans⁴  Robertson, Bengt² 

[1] Department of Clinical Chemistry, Karolinska Institutet at Danderyd Hospital, S-182 88 Danderyd, Stockholm, Sweden;Department of Pediatrics at St. Göran Hospital, S-112 81 Stockholm, Sweden;KabiGen AB, S-112 87 Stockholm Sweden;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Hydrophobic surfactant polypeptide;    Structural analysis;    Thioester;    Palmitoylation;   

DOI  :  10.1016/0014-5793(91)80373-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown