title: A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei.
abstract: The presence of the enzymatically active allergens equivalent to Der p I (cysteine protease), Der p III (serine protease) and amylase in extracts of Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei was determined using appropriate enzymatic techniques. Biochemical equivalents of all three allergens were present in each extract studied. Studies also showed that the mite extracts contained a variety of other biochemically active enzymes including trypsin, chymotrypsin, carboxypeptidase A and B, glucoamylase and lysozyme. Marked differences in the relative concentrations of some of these enzymes in different mite extracts were observed, particularly trypsin and carboxypeptidase A. The enzymes were physicochemically similar to equivalent enzymes from vertebrate and invertebrate sources. Chromatofocusing studies of faecal extracts derived from D. pteronyssinus and D. farinae showed that several isoforms of each enzyme were present. The data indicated that there were more trypsin isoforms, with pI over a wider range, in extracts prepared from D. pteronyssinus. Proteases and carbohydrases were also found in extracts prepared from faecally enriched material suggesting that they were endoperitrophic and associated with mite digestion. The data suggest that not only are the group I, III and amylase allergens a consistent feature of most pyroglyphid dust mites but also that other proteases and carbohydrases present in mite faeces are allergenic.
authors.affiliation: Western Australian Research Institute for Child Health, Princess Margaret Hospital, Subiaco, Perth.
authors.forename: G A
authors.initials: GA
authors.lastname: Stewart
authors.forename: C H
authors.initials: CH
authors.lastname: Bird
authors.forename: K D
authors.initials: KD
authors.lastname: Krska
authors.forename: M J
authors.initials: MJ
authors.lastname: Colloff
authors.forename: P J
authors.initials: PJ
authors.lastname: Thompson
mesh_terms: D000485:Allergens / Q000032:analysis*; D000681:Amylases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D000818:Animals; D010450:Endopeptidases / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D008925:Mites / Q000201:enzymology* / Q000276:immunology; D009113:Muramidase / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D013379:Substrate Specificity; D014357:Trypsin / Q000737:chemistry / Q000276:immunology / Q000378:metabolism
chemical_list: D000485:Allergens; D000681:Amylases; D006026:Glycoside Hydrolases; D009113:Muramidase; D005087:Glucan 1,4-alpha-Glucosidase; D010450:Endopeptidases; D014357:Trypsin