{"title":"新1-碳霉素LY163892 -内酰胺酶水解及抑制研究。","authors":"R N Jones, A L Barry","doi":"10.1007/BF02014248","DOIUrl":null,"url":null,"abstract":"<p><p>A novel 1-carbacephem, LY163892, was determined to be more stable to plasmid-mediated beta-lactamases than cefaclor. Chromosomal-mediated Type Ia and IVc enzymes destroyed LY163892 at rates ranging from 16 to 93% that of nitrocefin. LY163892 showed minimal ability to inhibit beta-lactamases other than Type Ia (P99).</p>","PeriodicalId":11958,"journal":{"name":"European Journal of Clinical Microbiology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1987-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02014248","citationCount":"6","resultStr":"{\"title\":\"Beta-lactamase hydrolysis and inhibition studies of the new 1-carbacephem LY163892.\",\"authors\":\"R N Jones, A L Barry\",\"doi\":\"10.1007/BF02014248\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A novel 1-carbacephem, LY163892, was determined to be more stable to plasmid-mediated beta-lactamases than cefaclor. Chromosomal-mediated Type Ia and IVc enzymes destroyed LY163892 at rates ranging from 16 to 93% that of nitrocefin. LY163892 showed minimal ability to inhibit beta-lactamases other than Type Ia (P99).</p>\",\"PeriodicalId\":11958,\"journal\":{\"name\":\"European Journal of Clinical Microbiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1987-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/BF02014248\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"European Journal of Clinical Microbiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/BF02014248\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"European Journal of Clinical Microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF02014248","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Beta-lactamase hydrolysis and inhibition studies of the new 1-carbacephem LY163892.
A novel 1-carbacephem, LY163892, was determined to be more stable to plasmid-mediated beta-lactamases than cefaclor. Chromosomal-mediated Type Ia and IVc enzymes destroyed LY163892 at rates ranging from 16 to 93% that of nitrocefin. LY163892 showed minimal ability to inhibit beta-lactamases other than Type Ia (P99).
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