Allergenicity and Physicochemical Characterization of House Dust Mite Derived Amylase | Zendy

Fiona Lake | Zendy; Larry D. Ward | Zendy; Richard J. Simpson | Zendy; Philip J. Thompson | Zendy; Geoffrey A. Stewart | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Allergenicity and Physicochemical Characterization of House Dust Mite Derived Amylase

Author(s) -

Fiona Lake,

Larry D. Ward,

Richard J. Simpson,

Philip J. Thompson,

Geoffrey A. Stewart

Publication year - 1991

Publication title -

international archives of allergy and immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.696

H-Index - 100

eISSN - 1423-0097

pISSN - 1018-2438

DOI - 10.1159/000235402

Subject(s) - mite , house dust mite , allergen , amylase , pyroglyphidae , enzyme , chemistry , immunology , biology , biochemistry , allergy , botany

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research