{"title":"锰缺乏症中不同脱氢酶和碱性磷酸酶的活性。","authors":"D Heiseke, M Kirchgessner","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The enzyme activities of the isocitrate, glucose-6-phosphate and malate dehydrogenases and of malic enzyme in liver, of lactate dehydrogenase in serum, and of alkaline phosphatase in bone and serum were determined in early-weaned rats given different Mn supplies. The activities of malate dehydrogenase were reduced by 16 and 18% during suboptimum and deficient Mn supply, respectively, the values of alkaline phosphatase in serum and bone were elevated by 29 and 35%, respectively. The enzyme values of the glucose-6-phosphate and lactate dehydrogenases were elevated only during Mn deficiency (by 40 and 65%, respectively), while a suboptimum Mn supply had no noticeable influence on these enzymes. The activities of isocitrate dehydrogenase and of malic enzyme, which were described to be activated by Mn++ in vitro, did not respond in vivo to Mn deficiency.</p>","PeriodicalId":19333,"journal":{"name":"Nutrition and metabolism","volume":"23 3","pages":"211-6"},"PeriodicalIF":0.0000,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Activity of different dehydrogenases and alkaline phosphatase in manganese deficiency].\",\"authors\":\"D Heiseke, M Kirchgessner\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The enzyme activities of the isocitrate, glucose-6-phosphate and malate dehydrogenases and of malic enzyme in liver, of lactate dehydrogenase in serum, and of alkaline phosphatase in bone and serum were determined in early-weaned rats given different Mn supplies. The activities of malate dehydrogenase were reduced by 16 and 18% during suboptimum and deficient Mn supply, respectively, the values of alkaline phosphatase in serum and bone were elevated by 29 and 35%, respectively. The enzyme values of the glucose-6-phosphate and lactate dehydrogenases were elevated only during Mn deficiency (by 40 and 65%, respectively), while a suboptimum Mn supply had no noticeable influence on these enzymes. The activities of isocitrate dehydrogenase and of malic enzyme, which were described to be activated by Mn++ in vitro, did not respond in vivo to Mn deficiency.</p>\",\"PeriodicalId\":19333,\"journal\":{\"name\":\"Nutrition and metabolism\",\"volume\":\"23 3\",\"pages\":\"211-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nutrition and metabolism\",\"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":"Nutrition and metabolism","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Activity of different dehydrogenases and alkaline phosphatase in manganese deficiency].
The enzyme activities of the isocitrate, glucose-6-phosphate and malate dehydrogenases and of malic enzyme in liver, of lactate dehydrogenase in serum, and of alkaline phosphatase in bone and serum were determined in early-weaned rats given different Mn supplies. The activities of malate dehydrogenase were reduced by 16 and 18% during suboptimum and deficient Mn supply, respectively, the values of alkaline phosphatase in serum and bone were elevated by 29 and 35%, respectively. The enzyme values of the glucose-6-phosphate and lactate dehydrogenases were elevated only during Mn deficiency (by 40 and 65%, respectively), while a suboptimum Mn supply had no noticeable influence on these enzymes. The activities of isocitrate dehydrogenase and of malic enzyme, which were described to be activated by Mn++ in vitro, did not respond in vivo to Mn deficiency.