F R Lake, L D Ward, R J Simpson, P J Thompson, G A Stewart
{"title":"Allergenicity and physicochemical characterization of house dust mite derived amylase.","authors":"F R Lake, L D Ward, R J Simpson, P J Thompson, G A Stewart","doi":"10.1159/000235402","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":13810,"journal":{"name":"International archives of allergy and applied immunology","volume":"94 1-4","pages":"357-8"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000235402","citationCount":"15","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International archives of allergy and applied immunology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000235402","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15
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.
淀粉酶被证明存在于从室内灰尘和用于培养翼状螨的废生长培养基中制备的提取物中。在灰尘中，它被证明与螨虫计数和粪便来源的螨虫过敏原Der p i的浓度相关。螨虫淀粉酶从培养基中分离出来，显示为分子量为56,000的单链蛋白。该酶含有游离巯基，其n端序列为KYXNPHFIGXRSVITXLME。使用对螨过敏的成人(46%阳性)和儿童(25%)的血清发现它是一种过敏原。致敏性的表达依赖于链内二硫键的完整性。
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