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。

R L Mellgren, K K Schlender
{"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,&nbsp;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,&nbsp;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}
引用次数: 0

摘要

用凝胶过滤层析法分离了兔肾皮质提取物的两种高分子量磷酸化酶和磷酸酶。两种热稳定抑制剂蛋白与磷酸酶峰共洗脱。磷酸化酶、磷酸酶和热稳定抑制剂的活性也在皮质提取物的凝胶电泳上共迁移。当提取物在凝胶过滤或电泳前加热到95度5分钟时,磷酸化酶磷酸酶抑制剂活性分别以较低的分子量和较高的迁移率洗脱。将皮质提取物在-20度下储存6个月,导致磷酸酶和抑制剂活性部分转化为低分子量形式,通过凝胶过滤共洗脱。对凝胶过滤色谱的两个抑制峰进行了热处理和表征。两个抑制剂峰的分子量均为25000 ~ 35000。其中一个峰的抑制活性通过环amp依赖性蛋白激酶和ATP孵育提高了约3.5倍,并且需要更高浓度的TCA沉淀。因此,其中一个抑制剂峰类似于兔肌肉抑制剂-1,而另一个峰可能代表类似于兔肌肉抑制剂-2的抑制剂。这些结果首次表明,低分子量热稳定抑制剂蛋白可能与细胞中高分子量磷酸化酶磷酸酶结合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信