Characterization and conformational analysis by Raman spectroscopy of human airway lysozyme.
Human airway lysozyme, purified from pathological bronchial secretions, is characterized by a specific activity 3-fold higher than that of hen egg-white lysozyme. The amino acid composition of human airway lysozyme is identical to that of other human lysozymes. The laser Raman spectra of human airway lysozyme and hen egg-white lysozyme in phosphate buffer solution (pH 7.2) are recorded in the range 300-1900 cm-1 at 488 nm. Drastic intensity differences are observed between the spectra analyzed in the ranges characteristic of the peptide backbone (e.g., beta-sheet; C alpha-C, C alpha-N), and of the aromatic side-chain vibrations (tyrosine, tryptophan). The deconvolution of the Raman amide I band gives secondary structures of 38% and 39% alpha-helix, 25% and 20% beta-sheet, and 37% and 41% undefined structure for the human and hen lysozymes, respectively.
J
J
Marx
J
J
Jacquot
M
M
Berjot
E
E
Puchelle
A J
AJ
Alix
D000596:Amino Acids / Q000032:analysis; D001980:Bronchi / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D009113:Muramidase / Q000032:analysis* / Q000378:metabolism; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
D000596:Amino Acids; D009113:Muramidase