{"title":"木糖氧化无色杆菌的磷脂酰胆碱特异性磷脂酶C。","authors":"A Ivanov, S Kostadinova","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A new phosphatidylcholine-specific phospholipase C (EC 3.1.4.3.) has been isolated from the culture broth of Achromobacter xylosoxidans. Growth conditions were optimized for maximum production of the enzyme. A temperature-sensitive synthesis was established. Chromatography on CM Sephadex and polyacrylamide gel electrophoresis of the native enzyme revealed a number of isozymes. The water soluble substrate for phospholipase p-nitrophenylphosphorylcholine was not hydrolysed by the enzyme.</p>","PeriodicalId":35526,"journal":{"name":"Acta Microbiologica Bulgarica","volume":"29 ","pages":"3-8"},"PeriodicalIF":0.0000,"publicationDate":"1993-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Phosphatidylcholine-specific phospholipase C from Achromobacter xylosoxidans.\",\"authors\":\"A Ivanov, S Kostadinova\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A new phosphatidylcholine-specific phospholipase C (EC 3.1.4.3.) has been isolated from the culture broth of Achromobacter xylosoxidans. Growth conditions were optimized for maximum production of the enzyme. A temperature-sensitive synthesis was established. Chromatography on CM Sephadex and polyacrylamide gel electrophoresis of the native enzyme revealed a number of isozymes. The water soluble substrate for phospholipase p-nitrophenylphosphorylcholine was not hydrolysed by the enzyme.</p>\",\"PeriodicalId\":35526,\"journal\":{\"name\":\"Acta Microbiologica Bulgarica\",\"volume\":\"29 \",\"pages\":\"3-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1993-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta Microbiologica Bulgarica\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Microbiologica Bulgarica","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
Phosphatidylcholine-specific phospholipase C from Achromobacter xylosoxidans.
A new phosphatidylcholine-specific phospholipase C (EC 3.1.4.3.) has been isolated from the culture broth of Achromobacter xylosoxidans. Growth conditions were optimized for maximum production of the enzyme. A temperature-sensitive synthesis was established. Chromatography on CM Sephadex and polyacrylamide gel electrophoresis of the native enzyme revealed a number of isozymes. The water soluble substrate for phospholipase p-nitrophenylphosphorylcholine was not hydrolysed by the enzyme.