{"title":"牛血小板磷脂酰肌醇特异性磷脂酶C。钙调素抑制剂的抑制作用——ATP和ADP的激活作用。","authors":"H Benedikter, G Knopki, P Renz","doi":"10.1515/znc-1985-1-214","DOIUrl":null,"url":null,"abstract":"<p><p>The phospholipase C-activity in crude extracts of bovine blood platelets is strongly inhibited by the calmodulin-inhibitors fluphenazine and calmidazolium in the mM range, and activated by ATP and ADP, but not by AMP. The activating effect is also shown by the nonhydrolysable ATP- and ADP-analogs alpha,beta- and beta,gamma-methyleneadenosine 5'-triphosphate and alpha,beta-methyleneadenosine 5'-diphosphate, thus indicating that it is an allosteric effect. The stimulation of the phospholipase C-activity by ATP is also detectable in some partially purified fractions of the crude platelet extract, but it is abolished on further purification of the enzyme.</p>","PeriodicalId":23914,"journal":{"name":"Zeitschrift fur Naturforschung. Section C, Biosciences","volume":"40 1-2","pages":"68-72"},"PeriodicalIF":0.0000,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znc-1985-1-214","citationCount":"0","resultStr":"{\"title\":\"Phosphatidylinositol-specific phospholipase C from bovine blood platelets. Inhibition by calmodulin-inhibitors--activation by ATP and ADP.\",\"authors\":\"H Benedikter, G Knopki, P Renz\",\"doi\":\"10.1515/znc-1985-1-214\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The phospholipase C-activity in crude extracts of bovine blood platelets is strongly inhibited by the calmodulin-inhibitors fluphenazine and calmidazolium in the mM range, and activated by ATP and ADP, but not by AMP. The activating effect is also shown by the nonhydrolysable ATP- and ADP-analogs alpha,beta- and beta,gamma-methyleneadenosine 5'-triphosphate and alpha,beta-methyleneadenosine 5'-diphosphate, thus indicating that it is an allosteric effect. The stimulation of the phospholipase C-activity by ATP is also detectable in some partially purified fractions of the crude platelet extract, but it is abolished on further purification of the enzyme.</p>\",\"PeriodicalId\":23914,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"volume\":\"40 1-2\",\"pages\":\"68-72\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1985-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znc-1985-1-214\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift fur Naturforschung. Section C, Biosciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/znc-1985-1-214\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift fur Naturforschung. Section C, Biosciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/znc-1985-1-214","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Phosphatidylinositol-specific phospholipase C from bovine blood platelets. Inhibition by calmodulin-inhibitors--activation by ATP and ADP.
The phospholipase C-activity in crude extracts of bovine blood platelets is strongly inhibited by the calmodulin-inhibitors fluphenazine and calmidazolium in the mM range, and activated by ATP and ADP, but not by AMP. The activating effect is also shown by the nonhydrolysable ATP- and ADP-analogs alpha,beta- and beta,gamma-methyleneadenosine 5'-triphosphate and alpha,beta-methyleneadenosine 5'-diphosphate, thus indicating that it is an allosteric effect. The stimulation of the phospholipase C-activity by ATP is also detectable in some partially purified fractions of the crude platelet extract, but it is abolished on further purification of the enzyme.
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