{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13"],"submitter":["Pytelkova J"],"pubmed_abstract":["<h4>Background</h4>Enzymatic allergens of storage mites that contaminate stored food products are poorly characterized. We describe biochemical and immunological properties of the native alpha-amylase allergen Aca s 4 from Acarus siro, a medically important storage mite.<h4>Results</h4>A. siro produced a high level of alpha-amylase activity attributed to Aca s 4. This enzyme was purified and identified by protein sequencing and LC-MS/MS analysis. Aca s 4 showed a distinct inhibition pattern and an unusual alpha-amylolytic activity with low sensitivity to activation by chloride ions. Homology modeling of Aca s 4 revealed a structural change in the chloride-binding site that may account for this activation pattern. Aca s 4 was recognized by IgE from house dust mite-sensitive patients, and po"],"journal":["BMC biochemistry"],"pagination":["3"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3306266"],"repository":["biostudies-literature"],"pubmed_title":["Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro."],"pmcid":["PMC3306266"],"pubmed_authors":["Sanda M","Mares M","Talacko P","Lepsik M","Pytelkova J","Maresova L"],"additional_accession":[]},"is_claimable":false,"name":"Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro.","description":"<h4>Background</h4>Enzymatic allergens of storage mites that contaminate stored food products are poorly characterized. We describe biochemical and immunological properties of the native alpha-amylase allergen Aca s 4 from Acarus siro, a medically important storage mite.<h4>Results</h4>A. siro produced a high level of alpha-amylase activity attributed to Aca s 4. This enzyme was purified and identified by protein sequencing and LC-MS/MS analysis. Aca s 4 showed a distinct inhibition pattern and an unusual alpha-amylolytic activity with low sensitivity to activation by chloride ions. Homology modeling of Aca s 4 revealed a structural change in the chloride-binding site that may account for this activation pattern. Aca s 4 was recognized by IgE from house dust mite-sensitive patients, and po","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Jan","modification":"2025-04-04T11:52:01.005Z","creation":"2019-03-27T00:51:15Z"},"accession":"S-EPMC3306266","cross_references":{"pubmed":["22292590"],"doi":["10.1186/1471-2091-13-3"]}}