{"title":"[甲状腺肌醇-1-磷酸合成酶(其纯化及特性)]。","authors":"H Stelmach, L Jaroszewicz","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Pig thyroid myoinositol-phosphate synthase was purified about 30 times using ammonium sulphate fractionation and DEAE cellulose chromatography. The enzyme preparation showed the activity of more than 70 mU/mg of protein. A partially purified synthase is a very labile enzyme. Its activity showed optimum value at pH 7.0. This activity appeared to be controlled by NH4+, Na+, and Li+ ions. The biological role of thyroid synthase has been discussed.</p>","PeriodicalId":77367,"journal":{"name":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","volume":"33-34 ","pages":"23-32"},"PeriodicalIF":0.0000,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Thyroid gland inositol-1-phosphate synthase (its purification and characteristics)].\",\"authors\":\"H Stelmach, L Jaroszewicz\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Pig thyroid myoinositol-phosphate synthase was purified about 30 times using ammonium sulphate fractionation and DEAE cellulose chromatography. The enzyme preparation showed the activity of more than 70 mU/mg of protein. A partially purified synthase is a very labile enzyme. Its activity showed optimum value at pH 7.0. This activity appeared to be controlled by NH4+, Na+, and Li+ ions. The biological role of thyroid synthase has been discussed.</p>\",\"PeriodicalId\":77367,\"journal\":{\"name\":\"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis\",\"volume\":\"33-34 \",\"pages\":\"23-32\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1988-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis\",\"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":"Roczniki Akademii Medycznej w Bialymstoku = Annales Academiae Medicae Bialostocensis","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Thyroid gland inositol-1-phosphate synthase (its purification and characteristics)].
Pig thyroid myoinositol-phosphate synthase was purified about 30 times using ammonium sulphate fractionation and DEAE cellulose chromatography. The enzyme preparation showed the activity of more than 70 mU/mg of protein. A partially purified synthase is a very labile enzyme. Its activity showed optimum value at pH 7.0. This activity appeared to be controlled by NH4+, Na+, and Li+ ions. The biological role of thyroid synthase has been discussed.