Physicochemical characterization of a major protein allergen, Der p I, from the house dust mite, Dermatophagoides pteronyssinus. Amino acid analysis and circular dichroism studies.
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.
D000485:Allergens / Q000302:isolation & purification*; D000596:Amino Acids; D000818:Animals; D039741:Antigens, Dermatophagoides; D002942:Circular Dichroism; D008925:Mites / Q000032:analysis*; D011487:Protein Conformation
D000485:Allergens; D000596:Amino Acids; D039741:Antigens, Dermatophagoides