Hydrophobic 3.7 kDa surfactant polypeptide: Structural characterization of the human and bovine forms

FEBS Letters

Christensen, Niels¹  Curstedt, Tore¹  Johansson, Jan¹  Eklund, Anders¹  Jörnvall, Hans¹  Robertson, Bengt¹ 

[1] Departments of Clinical Chemistry, Obstetrics and Gynecology, Thoracic Medicine at Karolinska Hospital, Pediatrics at St. Göran's Hospital and Chemistry I at Karolinska Institutet, Stockholm, Sweden

关键词: Surfactant;    Hydrophobic polypeptide;    Primary structure;    N-terminal trimming;    Species variation;   

DOI  :  10.1016/0014-5793(88)80386-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The human and bovine forms of the hydrophobic 3.7 kDa surfactant polypeptide have been structurally analyzed. The polypeptide is essentially inert to enzymatic proteolysis, and methods for analysis include peptide handling in organic solvents and fragment generation by limited acid hydrolysis. The molecule exhibits N-terminal trimming, and the relative abundance of the different starting positions varies both among species and between adult and fetal forms of the surfactant polypeptide. The bovine major form is one residue shorter than the mature 35-residue human molecule. Comparison of the porcine, human and bovine polypeptides reveals a conserved hydrophobic middle/C-terminal segment and a variable hydrophilic N-terminal part.

【 授权许可】

Unknown