Far-UV CD spectroscopy, IR spectroscopy, and immunological properties of synthetic peptides, including an amphipathic alpha-helical peptide from bovine phospholipase A2.
The immunological properties of bovine phospholipase A2 were investigated in order to locate possible sequential epitopes. Polyvalent antiserum raised against the enzyme was tested for its interaction with synthetic peptides derived from regions adopting hydrogen-bonded secondary structures within the tertiary structure of phospholipase A2. The conformations of each peptide in various solvents were determined by CD and ir spectroscopy in order to relate immunological to structural properties. It was found that sequential epitopes are absent in this enzyme, but that region 90-109 could be a possible T-cell epitope through the formation of an amphipathic alpha-helix.
Division of Processing and Chemical Manufacturing Technology, CSIR, Pretoria, Republic of South Africa.
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D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D000939:Epitopes / Q000032:analysis; D006168:Guinea Pigs; D007106:Immune Sera / Q000276:immunology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology*; D010740:Phospholipases / Q000276:immunology*; D010741:Phospholipases A / Q000276:immunology*; D054467:Phospholipases A2; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet
D000939:Epitopes; D007106:Immune Sera; D010446:Peptide Fragments; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2