{"title":"[革兰氏阴性菌氨基糖苷转移酶的繁殖]。","authors":"B Wiedemann, G Tetzlaff, U van Treeck","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Molecular genetic and enzymatic studies on Gram-negative bacteria from hospital specimens give the following picture on surveillance of aminoglycoside transferases: The most frequent enzymes inactivate streptomycin only, AAD- (3'') and APH-(3''). Only 15% of the isolated enzymes inactivate gentamycin, tobramycin, sisomycin or amikacin. The most frequent of these are AAD-(2'') with 7% and AAC-(6') IV with 3%, both enzymes inactivate a wide range of substrates. The high frequency of streptomycin inactivating enzymes is due to the high incidence of linked resistance markers. A plasmid rPB1 is described, that is present in about 10% of all clinical isolates of E. coli. It has a molecular weight of 4. 1 Mdal and typical restriction pattern.</p>","PeriodicalId":75937,"journal":{"name":"International journal of clinical pharmacology and biopharmacy","volume":"17 3","pages":"138-44"},"PeriodicalIF":0.0000,"publicationDate":"1979-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[The propagation of aminoglycoside transferases in gram negative bacteria].\",\"authors\":\"B Wiedemann, G Tetzlaff, U van Treeck\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Molecular genetic and enzymatic studies on Gram-negative bacteria from hospital specimens give the following picture on surveillance of aminoglycoside transferases: The most frequent enzymes inactivate streptomycin only, AAD- (3'') and APH-(3''). Only 15% of the isolated enzymes inactivate gentamycin, tobramycin, sisomycin or amikacin. The most frequent of these are AAD-(2'') with 7% and AAC-(6') IV with 3%, both enzymes inactivate a wide range of substrates. The high frequency of streptomycin inactivating enzymes is due to the high incidence of linked resistance markers. A plasmid rPB1 is described, that is present in about 10% of all clinical isolates of E. coli. It has a molecular weight of 4. 1 Mdal and typical restriction pattern.</p>\",\"PeriodicalId\":75937,\"journal\":{\"name\":\"International journal of clinical pharmacology and biopharmacy\",\"volume\":\"17 3\",\"pages\":\"138-44\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International journal of clinical pharmacology and biopharmacy\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International journal of clinical pharmacology and biopharmacy","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[The propagation of aminoglycoside transferases in gram negative bacteria].
Molecular genetic and enzymatic studies on Gram-negative bacteria from hospital specimens give the following picture on surveillance of aminoglycoside transferases: The most frequent enzymes inactivate streptomycin only, AAD- (3'') and APH-(3''). Only 15% of the isolated enzymes inactivate gentamycin, tobramycin, sisomycin or amikacin. The most frequent of these are AAD-(2'') with 7% and AAC-(6') IV with 3%, both enzymes inactivate a wide range of substrates. The high frequency of streptomycin inactivating enzymes is due to the high incidence of linked resistance markers. A plasmid rPB1 is described, that is present in about 10% of all clinical isolates of E. coli. It has a molecular weight of 4. 1 Mdal and typical restriction pattern.