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Comparative Study
. 1992 Nov;16(1-2):165-80.
doi: 10.1007/BF01201499.

A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei

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Comparative Study

A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei

G A Stewart et al. Exp Appl Acarol. 1992 Nov.

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.

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References

    1. J Allergy Clin Immunol. 1986 Jan;77(1 Pt 1):14-24 - PubMed
    1. Clin Exp Allergy. 1991 Jan;21(1):25-32 - PubMed
    1. Q J Microsc Sci. 1950 Mar;91(1):45-61 - PubMed
    1. J Allergy Clin Immunol. 1987 Jan;79(1):93-102 - PubMed
    1. Anal Biochem. 1985 May 1;146(2):353-60 - PubMed

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