Physicochemical Characterization of a Major Protein Allergen, Derp I, from the House Dust Mite, Dermatophagoides pteronyssinus
Geoffrey A. Stewart, Richard J. Simpson, Wayne Robert Thomas, Keven J. Turner
Abstract
Geoffrey A. Stewart, Richard J. Simpson, Wayne Robert Thomas, Keven J. Turner
Abstract
A major house dust mite allergen, Der p I, was isolated from spent growth medium and physicochemically characterized. These studies show that the allergen is monomeric, contains approximately 216 residues and 4 intra-chain disulphide bonds. The N-terminal amino acid is threonine. Circular dichroism studies show that the allergen contains 10% alpha-helical, 50% beta-pleated sheet and 40% random structures.
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A major house dust mite allergen, Der p I, was isolated from spent growth medium and physicochemically characterized. These studies show that the allergen is monomeric, contains approximately 216 residues and 4 intra-chain disulphide bonds. The N-terminal amino acid is threonine. Circular dichroism studies show that the allergen contains 10% alpha-helical, 50% beta-pleated sheet and 40% random structures.
Key concepts: Allergen, House dust mite, Circular dichroism, Chemistry, Pyroglyphidae, Monomer, Threonine, Immunology