{"title":"兔肾皮质磷酸化酶磷酸酶:高分子量形式和热稳定抑制剂蛋白之间复合物的证据。","authors":"R L Mellgren, K K Schlender","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Two forms of high molecular weight phosphorylase phosphatase have been partially resolved by gel filtration chromatography of rabbit kidney cortex extracts. Two heat-stable inhibitor proteins co-eluted with the phosphatase peaks. Phosphorylase phosphatase and heat-stable inhibitor activity also co-migrated on gel electrophoresis of cortex extracts. When extracts were heated to 95 degrees for 5 minutes prior to gel filtration or electrophoresis, phosphorylase phosphatase inhibitor activity eluted at a lower molecular weight and a higher mobility, respectively. Storing cortex extracts at -20 degrees for 6 months resulted in partial conversion of both phosphatase and inhibitor activities to lower molecular weight forms which co-eluted on gel filtration. The two inhibitor peaks from gel filtration chromatography were heat-treated and characterized. Both inhibitor peaks had molecular weight of 25,000 to 35,000. The inhibitory activity of one of the peaks was increased about 3.5-fold by incubation with cyclic AMP-dependent protein kinase and ATP, and required higher concentrations of TCA to be precipitated. Hence, one of the inhibitor peaks resembled rabbit muscle inhibitor -1, while the other peak may represent an inhibitor similar to rabbit muscle inhibitor -2. These results represent the first indication that low molecular weight heat-stable inhibitor proteins may be bound to high molecular weight phosphorylase phosphatases in the cell.</p>","PeriodicalId":15497,"journal":{"name":"Journal of cyclic nucleotide research","volume":"8 1","pages":"27-37"},"PeriodicalIF":0.0000,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Rabbit kidney cortex phosphorylase phosphatases: evidence for complexes between high molecular weight forms and heat-stable inhibitor proteins.\",\"authors\":\"R L Mellgren, K K Schlender\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Two forms of high molecular weight phosphorylase phosphatase have been partially resolved by gel filtration chromatography of rabbit kidney cortex extracts. Two heat-stable inhibitor proteins co-eluted with the phosphatase peaks. Phosphorylase phosphatase and heat-stable inhibitor activity also co-migrated on gel electrophoresis of cortex extracts. When extracts were heated to 95 degrees for 5 minutes prior to gel filtration or electrophoresis, phosphorylase phosphatase inhibitor activity eluted at a lower molecular weight and a higher mobility, respectively. Storing cortex extracts at -20 degrees for 6 months resulted in partial conversion of both phosphatase and inhibitor activities to lower molecular weight forms which co-eluted on gel filtration. The two inhibitor peaks from gel filtration chromatography were heat-treated and characterized. Both inhibitor peaks had molecular weight of 25,000 to 35,000. The inhibitory activity of one of the peaks was increased about 3.5-fold by incubation with cyclic AMP-dependent protein kinase and ATP, and required higher concentrations of TCA to be precipitated. Hence, one of the inhibitor peaks resembled rabbit muscle inhibitor -1, while the other peak may represent an inhibitor similar to rabbit muscle inhibitor -2. These results represent the first indication that low molecular weight heat-stable inhibitor proteins may be bound to high molecular weight phosphorylase phosphatases in the cell.</p>\",\"PeriodicalId\":15497,\"journal\":{\"name\":\"Journal of cyclic nucleotide research\",\"volume\":\"8 1\",\"pages\":\"27-37\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1982-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of cyclic nucleotide 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 research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Rabbit kidney cortex phosphorylase phosphatases: evidence for complexes between high molecular weight forms and heat-stable inhibitor proteins.
Two forms of high molecular weight phosphorylase phosphatase have been partially resolved by gel filtration chromatography of rabbit kidney cortex extracts. Two heat-stable inhibitor proteins co-eluted with the phosphatase peaks. Phosphorylase phosphatase and heat-stable inhibitor activity also co-migrated on gel electrophoresis of cortex extracts. When extracts were heated to 95 degrees for 5 minutes prior to gel filtration or electrophoresis, phosphorylase phosphatase inhibitor activity eluted at a lower molecular weight and a higher mobility, respectively. Storing cortex extracts at -20 degrees for 6 months resulted in partial conversion of both phosphatase and inhibitor activities to lower molecular weight forms which co-eluted on gel filtration. The two inhibitor peaks from gel filtration chromatography were heat-treated and characterized. Both inhibitor peaks had molecular weight of 25,000 to 35,000. The inhibitory activity of one of the peaks was increased about 3.5-fold by incubation with cyclic AMP-dependent protein kinase and ATP, and required higher concentrations of TCA to be precipitated. Hence, one of the inhibitor peaks resembled rabbit muscle inhibitor -1, while the other peak may represent an inhibitor similar to rabbit muscle inhibitor -2. These results represent the first indication that low molecular weight heat-stable inhibitor proteins may be bound to high molecular weight phosphorylase phosphatases in the cell.