{"title":"黑根霉NRRL 1477的11 α和17 α -孕酮羟化酶。","authors":"A M Allam, I A el-Kady","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Differential induction of cultures of Rhizopus nigricans indicated that hydroxylation of progesterone at the 11alpha- and 17alpha-positions is due to two separate enzymes. This is supported by the finding that 11alpha- and 17alpha-hydroxylating activities are separated by differential centrigufation of cell-free extracts. The feasibility of introducing a hydroxyl group at the 11alpha- or 17alpha-position of hydroxylated progesterone derivatives was tested.</p>","PeriodicalId":75389,"journal":{"name":"Acta microbiologica Polonica. Series A: Microbiologia generalis","volume":"7 1","pages":"41-4"},"PeriodicalIF":0.0000,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The 11alpha and 17alpha-progesterone hydroxylases of Rhizopus nigricans NRRL 1477.\",\"authors\":\"A M Allam, I A el-Kady\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Differential induction of cultures of Rhizopus nigricans indicated that hydroxylation of progesterone at the 11alpha- and 17alpha-positions is due to two separate enzymes. This is supported by the finding that 11alpha- and 17alpha-hydroxylating activities are separated by differential centrigufation of cell-free extracts. The feasibility of introducing a hydroxyl group at the 11alpha- or 17alpha-position of hydroxylated progesterone derivatives was tested.</p>\",\"PeriodicalId\":75389,\"journal\":{\"name\":\"Acta microbiologica Polonica. Series A: Microbiologia generalis\",\"volume\":\"7 1\",\"pages\":\"41-4\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1975-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta microbiologica Polonica. Series A: Microbiologia generalis\",\"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":"Acta microbiologica Polonica. Series A: Microbiologia generalis","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The 11alpha and 17alpha-progesterone hydroxylases of Rhizopus nigricans NRRL 1477.
Differential induction of cultures of Rhizopus nigricans indicated that hydroxylation of progesterone at the 11alpha- and 17alpha-positions is due to two separate enzymes. This is supported by the finding that 11alpha- and 17alpha-hydroxylating activities are separated by differential centrigufation of cell-free extracts. The feasibility of introducing a hydroxyl group at the 11alpha- or 17alpha-position of hydroxylated progesterone derivatives was tested.
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