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Allergenicity and physicochemical characterization of house dust mite derived amylase.

Authors :
Lake FR
Ward LD
Simpson RJ
Thompson PJ
Stewart GA
Source :
International archives of allergy and applied immunology [Int Arch Allergy Appl Immunol] 1991; Vol. 94 (1-4), pp. 357-8.
Publication Year :
1991

Abstract

The enzyme amylase was shown to be present in extracts prepared from both house dust and spent growth medium used in the culture of the mite Dermatophagoides pteronyssinus. In dust, it was shown to correlate with both mite counts and concentrations of the faecally derived mite allergen, Der p I. Mite amylase was isolated from the culture medium and shown to be a single chain protein with a molecular weight of 56,000. The enzyme contained free sulphydryl groups and had the N-terminal sequence, KYXNPHFIGXRSVITXLME. It was found to be an allergen using sera from adults (46% positive) and children (25%) who were mite allergic. The expression of allergenicity was dependent on the integrity of intra-chain disulphide bonds.

Details

Language :
English
ISSN :
0020-5915
Volume :
94
Issue :
1-4
Database :
MEDLINE
Journal :
International archives of allergy and applied immunology
Publication Type :
Academic Journal
Accession number :
1718897
Full Text :
https://doi.org/10.1159/000235402