2009•International Archives of Allergy and Applied ImmunologyRequires access

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

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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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What this paper is about

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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Available 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.

Key concepts: Allergen, House dust mite, Circular dichroism, Chemistry, Pyroglyphidae, Monomer, Threonine, Immunology

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Physicochemical Characterization of a Major Protein Allergen, Derp I, from the House Dust Mite, Dermatophagoides pteronyssinus — Research Paper | ScholarLens