{"title":"Faecally derived hydrolytic enzymes from Dermatophagoides pteronyssinus: physicochemical characterisation of potential allergens.","authors":"G A Stewart, F R Lake, P J Thompson","doi":"10.1159/000235437","DOIUrl":null,"url":null,"abstract":"<p><p>The previous findings that the group I and III mite allergens, and amylase present in mite faeces are hydrolytic enzymes has prompted a study to determine whether this material contains other enzymes which could be allergenic. Thus, spent growth medium devoid of whole Dermatophagoides pteronyssinus mites was shown to contain glucoamylase, lipase and lysozyme in addition to the cysteine protease, serine protease and amylase activities associated with the above allergens, respectively. All of these enzymes are probably associated with mite digestive processes. They were rapidly solubilised, heterogeneous with regard to charge (pI in the range 4-8) and demonstrated maximum biochemical activity in the neutral pH range. Three serine proteases were detected and comprised a chymotrypsin-like, a trypsin-like and an unclassified enzyme with pI of 4.1 and 5.3, 8.5 and 7.1, respectively. Only one cysteine protease was observed, which paralleled immunochemically identified Der p I in a variety of assays. It was shown to cleave at lysyl residues and could be inhibited by the specific cysteine protease inhibitor, E-64. The remaining serine proteases, glucoamylase, lipase and lysozyme represent potential allergens.</p>","PeriodicalId":13810,"journal":{"name":"International archives of allergy and applied immunology","volume":"95 2-3","pages":"248-56"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000235437","citationCount":"77","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International archives of allergy and applied immunology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000235437","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 77
Abstract
The previous findings that the group I and III mite allergens, and amylase present in mite faeces are hydrolytic enzymes has prompted a study to determine whether this material contains other enzymes which could be allergenic. Thus, spent growth medium devoid of whole Dermatophagoides pteronyssinus mites was shown to contain glucoamylase, lipase and lysozyme in addition to the cysteine protease, serine protease and amylase activities associated with the above allergens, respectively. All of these enzymes are probably associated with mite digestive processes. They were rapidly solubilised, heterogeneous with regard to charge (pI in the range 4-8) and demonstrated maximum biochemical activity in the neutral pH range. Three serine proteases were detected and comprised a chymotrypsin-like, a trypsin-like and an unclassified enzyme with pI of 4.1 and 5.3, 8.5 and 7.1, respectively. Only one cysteine protease was observed, which paralleled immunochemically identified Der p I in a variety of assays. It was shown to cleave at lysyl residues and could be inhibited by the specific cysteine protease inhibitor, E-64. The remaining serine proteases, glucoamylase, lipase and lysozyme represent potential allergens.
先前发现螨虫粪便中的I类和III类过敏原和淀粉酶是水解酶,这促使人们进行研究,以确定该物质是否含有其他可能致敏的酶。由此可见,除含有与上述过敏原相关的半胱氨酸蛋白酶、丝氨酸蛋白酶和淀粉酶活性外,不含整只翼螨的生长培养基中还含有葡萄糖淀粉酶、脂肪酶和溶菌酶。所有这些酶都可能与螨虫的消化过程有关。它们溶解迅速,电荷不均匀(pI在4-8范围内),在中性pH范围内表现出最大的生化活性。检测到3种丝氨酸蛋白酶,分别由胰凝乳蛋白酶样酶、胰蛋白酶样酶和未分类酶组成,pI分别为4.1和5.3、8.5和7.1。仅观察到一种半胱氨酸蛋白酶,在各种检测中与免疫化学鉴定的Der p I相似。结果表明,它能在赖氨酸残基处裂解,并能被特异性半胱氨酸蛋白酶抑制剂E-64抑制。剩余的丝氨酸蛋白酶、葡萄糖淀粉酶、脂肪酶和溶菌酶是潜在的过敏原。