{"title":"腺苷酸环化酶活性与福斯克林浓度的关系。","authors":"R Barber, T J Goka","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The activation of adenylate cyclase by forskolin was investigated in terms of the dissociation model of guanyl nucleotide binding protein (Ns). It was demonstrated that the biphasic forskolin concentration-response of adenylate cyclase could be explained by the dissociation of the beta subunit. The equations developed from such a theoretical approach gave an accurate description of concentration response data from S49 cultured mouse lymphoma cells.</p>","PeriodicalId":15406,"journal":{"name":"Journal of cyclic nucleotide and protein phosphorylation research","volume":"10 1","pages":"23-9"},"PeriodicalIF":0.0000,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Adenylate cyclase activity as a function of forskolin concentration.\",\"authors\":\"R Barber, T J Goka\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The activation of adenylate cyclase by forskolin was investigated in terms of the dissociation model of guanyl nucleotide binding protein (Ns). It was demonstrated that the biphasic forskolin concentration-response of adenylate cyclase could be explained by the dissociation of the beta subunit. The equations developed from such a theoretical approach gave an accurate description of concentration response data from S49 cultured mouse lymphoma cells.</p>\",\"PeriodicalId\":15406,\"journal\":{\"name\":\"Journal of cyclic nucleotide and protein phosphorylation research\",\"volume\":\"10 1\",\"pages\":\"23-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1985-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of cyclic nucleotide and protein phosphorylation research\",\"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":"Journal of cyclic nucleotide and protein phosphorylation research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Adenylate cyclase activity as a function of forskolin concentration.
The activation of adenylate cyclase by forskolin was investigated in terms of the dissociation model of guanyl nucleotide binding protein (Ns). It was demonstrated that the biphasic forskolin concentration-response of adenylate cyclase could be explained by the dissociation of the beta subunit. The equations developed from such a theoretical approach gave an accurate description of concentration response data from S49 cultured mouse lymphoma cells.
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