{"title":"噬菌体T4幽灵的溶菌酶活性","authors":"B. Szewczyk, R. Skórko","doi":"10.1016/0005-2744(81)90233-3","DOIUrl":null,"url":null,"abstract":"<div><p>Bacteriophage T4 ghosts were found to possess lysozyme (mucopeptide <em>N</em>-acetylmuramoylhydrolase, EC 3.2.1. 17) activity. This enzyme is probably responsible for the lysis from without, observed at high multiplicity of infection, a process independent of the presence of the <em>e</em> gene product which is also a lysozyme. The ghost lysozyme and <em>e</em> lysozyme differed with respect to their requirements for maximal catalytic activity and to some extent in substrate specificity. The ghost lysozyme was released from phase particle by the action of Triton X-100.</p></div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":"662 1","pages":"Pages 131-137"},"PeriodicalIF":0.0000,"publicationDate":"1981-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90233-3","citationCount":"7","resultStr":"{\"title\":\"Lysozyme activity of bacteriophage T4 ghosts\",\"authors\":\"B. Szewczyk, R. Skórko\",\"doi\":\"10.1016/0005-2744(81)90233-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Bacteriophage T4 ghosts were found to possess lysozyme (mucopeptide <em>N</em>-acetylmuramoylhydrolase, EC 3.2.1. 17) activity. This enzyme is probably responsible for the lysis from without, observed at high multiplicity of infection, a process independent of the presence of the <em>e</em> gene product which is also a lysozyme. The ghost lysozyme and <em>e</em> lysozyme differed with respect to their requirements for maximal catalytic activity and to some extent in substrate specificity. The ghost lysozyme was released from phase particle by the action of Triton X-100.</p></div>\",\"PeriodicalId\":100159,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology\",\"volume\":\"662 1\",\"pages\":\"Pages 131-137\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-11-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2744(81)90233-3\",\"citationCount\":\"7\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005274481902333\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005274481902333","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Bacteriophage T4 ghosts were found to possess lysozyme (mucopeptide N-acetylmuramoylhydrolase, EC 3.2.1. 17) activity. This enzyme is probably responsible for the lysis from without, observed at high multiplicity of infection, a process independent of the presence of the e gene product which is also a lysozyme. The ghost lysozyme and e lysozyme differed with respect to their requirements for maximal catalytic activity and to some extent in substrate specificity. The ghost lysozyme was released from phase particle by the action of Triton X-100.
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