{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T14:11:21Z","timestamp":1791036681450,"version":"4.1.0"},"reference-count":34,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2008,4,25]],"date-time":"2008-04-25T00:00:00Z","timestamp":1209081600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Allergy"],"published-print":{"date-parts":[[2008,6]]},"abstract":"<jats:p><jats:bold>Background:\u00a0<\/jats:bold> Cockroach allergens are associated with the development of asthma, but none of these has been characterized for proteolytic activity. This study was undertaken to isolate and characterize a protease from <jats:italic>Periplaneta americana<\/jats:italic> and determine its allergenicity.<\/jats:p><jats:p><jats:bold>Methods:\u00a0<\/jats:bold> A serine protease was isolated from <jats:italic>P. americana<\/jats:italic> extract using benzamidine sepharose column and characterized by immunobiochemical methods. Allergenicity of the protease was assessed by enzyme\u2010linked immunosorbent assay, immunoblot, intradermal testing, histamine release and peripheral blood mononuclear cells (PBMCs) proliferation.<\/jats:p><jats:p><jats:bold>Results:\u2002<\/jats:bold> Affinity purified protein of \u223c28\u2003kDa (Per a 10) showed a single band of activity in gelatin zymogram and agarose plate assay. N\u2010terminal sequence (IVGGRPAQI) revealed similarity with mite serine protease allergens and insect trypsins. It demonstrated proteolytic activity with azocollagen\u2003&gt;\u2003gelatin\u2003&gt;\u2003defatted\u2010milk\u2003&gt;\u2003casein including serine protease specific substrate, <jats:italic>N<\/jats:italic>\u2010benzoyl\u2010arginine\u2010ethyl\u2010ester\u2010hydrochloride. It was inhibited by serine protease inhibitors, namely aprotinin\u2003&gt;\u2003pefabloc\u2003&gt;\u2003AEBSF\u2003&gt;\u2003PMSF\u2003&gt; benzamidine\u2003&gt;\u2003antipain\u2003&gt;\u2003leupeptin and trypsin\u2010specific inhibitor (tosyl\u2010lysyl\u2010chloromethyl\u2010ketone) suggesting it to be a trypsin\u2010like serine protease. Per a 10 was recognized as a major allergen, showing IgE reactivity with &gt;80% of cockroach sensitized patients by skin tests and immunoblot. It could induce significant histamine release (<jats:italic>P\u2003<\/jats:italic>&lt;\u20030.05) in blood and secretion of interleukin\u20104 (IL\u20104) (<jats:italic>P\u2003<\/jats:italic>&lt;\u20030.05) and IL\u20105 (<jats:italic>P\u2003<\/jats:italic>&lt;\u20030.05) in culture supernatant of PBMCs from cockroach hypersensitive patients, suggesting a strong allergenic potency.<\/jats:p><jats:p><jats:bold>Conclusion:\u00a0<\/jats:bold> A serine protease isolated from <jats:italic>P. americana<\/jats:italic> was demonstrated to be a major allergen (Per a 10). It has a potential for component\u2010based diagnosis of allergy and will be useful in elucidating the mechanism of allergy.<\/jats:p>","DOI":"10.1111\/j.1398-9995.2007.01602.x","type":"journal-article","created":{"date-parts":[[2008,4,25]],"date-time":"2008-04-25T13:45:45Z","timestamp":1209131145000},"page":"768-776","source":"Crossref","is-referenced-by-count":96,"title":["Identification of a serine protease as a major allergen (Per a 10) of <i>Periplaneta americana<\/i>"],"prefix":"10.1111","volume":"63","author":[{"given":"V. T.","family":"Sudha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N.","family":"Arora","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S. 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