<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>13</volume><submitter>Pytelkova J</submitter><pubmed_abstract>&lt;h4>Background&lt;/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.&lt;h4>Results&lt;/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</pubmed_abstract><journal>BMC biochemistry</journal><pagination>3</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3306266</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro.</pubmed_title><pmcid>PMC3306266</pmcid><pubmed_authors>Sanda M</pubmed_authors><pubmed_authors>Mares M</pubmed_authors><pubmed_authors>Talacko P</pubmed_authors><pubmed_authors>Lepsik M</pubmed_authors><pubmed_authors>Pytelkova J</pubmed_authors><pubmed_authors>Maresova L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro.</name><description>&lt;h4>Background&lt;/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.&lt;h4>Results&lt;/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</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Jan</publication><modification>2025-04-04T11:52:01.005Z</modification><creation>2019-03-27T00:51:15Z</creation></dates><accession>S-EPMC3306266</accession><cross_references><pubmed>22292590</pubmed><doi>10.1186/1471-2091-13-3</doi></cross_references></HashMap>