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Hydrophobic 3.7 kDa surfactant polypeptide: Structural characterization of the human and bovine forms
Author(s) -
Johansson Jan,
Jörnvall Hans,
Eklund Anders,
Christensen Niels,
Robertson Bengt,
Curstedt Tore
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80386-7
Subject(s) - pulmonary surfactant , chemistry , characterization (materials science) , biochemistry , biophysics , chromatography , materials science , nanotechnology , biology
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.