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Allergenicity and physicochemical characterization of house dust mite derived amylase.

Authors
  • Lake, F R
  • Ward, L D
  • Simpson, R J
  • Thompson, P J
  • Stewart, G A
Type
Published Article
Journal
International archives of allergy and applied immunology
Publication Date
Jan 01, 1991
Volume
94
Issue
1-4
Pages
357–358
Identifiers
PMID: 1718897
Source
Medline
License
Unknown

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.

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