{"title":"[完整大鼠和Zaidel腹水型肝癌大鼠肝组织葡萄糖-6-磷酸脱氢酶的性质]。","authors":"L S Chesnokova","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The properties of glucose-6-phosphate dehydrogenase (G6PDH; glucose-6-phosphate-NADP-oxidoreductase, EC 1.1.1.49) in the liver tissue of intact rats and those with ascites Zaidel hepatoma were compared. The specific activity of the enzyme from hepatoma was 7 times as high as that of the enzyme from the normal liver. The G6PDH preparations with the specific activity of 1.5 U/mg of protein were obtained by the three-stage purification. No differences in kinetic properties, coenzyme specificity and electrophoretic mobility of the enzymes from hepatoma and normal liver were observed.</p>","PeriodicalId":77530,"journal":{"name":"Eksperimental'naia onkologiia","volume":"12 3","pages":"68-70"},"PeriodicalIF":0.0000,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Properties of glucose-6-phosphate dehydrogenase of the liver tissue of intact rats and rats with Zaidel ascitic hepatoma].\",\"authors\":\"L S Chesnokova\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The properties of glucose-6-phosphate dehydrogenase (G6PDH; glucose-6-phosphate-NADP-oxidoreductase, EC 1.1.1.49) in the liver tissue of intact rats and those with ascites Zaidel hepatoma were compared. The specific activity of the enzyme from hepatoma was 7 times as high as that of the enzyme from the normal liver. The G6PDH preparations with the specific activity of 1.5 U/mg of protein were obtained by the three-stage purification. No differences in kinetic properties, coenzyme specificity and electrophoretic mobility of the enzymes from hepatoma and normal liver were observed.</p>\",\"PeriodicalId\":77530,\"journal\":{\"name\":\"Eksperimental'naia onkologiia\",\"volume\":\"12 3\",\"pages\":\"68-70\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Eksperimental'naia onkologiia\",\"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":"Eksperimental'naia onkologiia","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Properties of glucose-6-phosphate dehydrogenase of the liver tissue of intact rats and rats with Zaidel ascitic hepatoma].
The properties of glucose-6-phosphate dehydrogenase (G6PDH; glucose-6-phosphate-NADP-oxidoreductase, EC 1.1.1.49) in the liver tissue of intact rats and those with ascites Zaidel hepatoma were compared. The specific activity of the enzyme from hepatoma was 7 times as high as that of the enzyme from the normal liver. The G6PDH preparations with the specific activity of 1.5 U/mg of protein were obtained by the three-stage purification. No differences in kinetic properties, coenzyme specificity and electrophoretic mobility of the enzymes from hepatoma and normal liver were observed.
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