{"title":"猪心脏潜伏蛋白磷酸酶的纯化。","authors":"M D Schuchard, S D Killilea","doi":"10.1080/10826069208021371","DOIUrl":null,"url":null,"abstract":"<p><p>Latent protein phosphatase, Fc.M, was purified from porcine heart extracts by a procedure involving precipitation at pH 5.0, DEAE-Sephacel chromatography, ammonium sulfate fractionation, chromatography on phenyl-Sepharose, Biogel-A 0.5m and poly-L-lysine-agarose. The purified enzyme had a specific activity of 12,200 nanomoles of phosphate released from phosphorylase a/mg protein when assayed following activation by pretreatment with Mn++ and trypsin in the presence of 0.2 M NaCl. The enzyme is a heterodimer of 66 kDa composed of a catalytic (37 kDa) and a modulator (31 kDa) subunit.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"22 3-4","pages":"199-213"},"PeriodicalIF":0.0000,"publicationDate":"1992-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069208021371","citationCount":"1","resultStr":"{\"title\":\"Purification of porcine heart latent protein phosphatase Fc.M.\",\"authors\":\"M D Schuchard, S D Killilea\",\"doi\":\"10.1080/10826069208021371\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Latent protein phosphatase, Fc.M, was purified from porcine heart extracts by a procedure involving precipitation at pH 5.0, DEAE-Sephacel chromatography, ammonium sulfate fractionation, chromatography on phenyl-Sepharose, Biogel-A 0.5m and poly-L-lysine-agarose. The purified enzyme had a specific activity of 12,200 nanomoles of phosphate released from phosphorylase a/mg protein when assayed following activation by pretreatment with Mn++ and trypsin in the presence of 0.2 M NaCl. The enzyme is a heterodimer of 66 kDa composed of a catalytic (37 kDa) and a modulator (31 kDa) subunit.</p>\",\"PeriodicalId\":20391,\"journal\":{\"name\":\"Preparative biochemistry\",\"volume\":\"22 3-4\",\"pages\":\"199-213\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1992-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/10826069208021371\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Preparative biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/10826069208021371\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Preparative biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10826069208021371","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
摘要
潜伏蛋白磷酸酶经pH 5.0沉淀、DEAE-Sephacel层析、硫酸铵分馏、苯基- sepharose层析、Biogel-A 0.5m层析和聚l-赖氨酸-琼脂糖层析，从猪心脏提取物中纯化出M。在0.2 M NaCl的作用下，用Mn++和胰蛋白酶预处理磷酸化酶a释放的磷酸比活性为12200纳米摩尔/mg蛋白。该酶是由催化亚基(37 kDa)和调节亚基(31 kDa)组成的异二聚体，分子量为66 kDa。
Purification of porcine heart latent protein phosphatase Fc.M.
Latent protein phosphatase, Fc.M, was purified from porcine heart extracts by a procedure involving precipitation at pH 5.0, DEAE-Sephacel chromatography, ammonium sulfate fractionation, chromatography on phenyl-Sepharose, Biogel-A 0.5m and poly-L-lysine-agarose. The purified enzyme had a specific activity of 12,200 nanomoles of phosphate released from phosphorylase a/mg protein when assayed following activation by pretreatment with Mn++ and trypsin in the presence of 0.2 M NaCl. The enzyme is a heterodimer of 66 kDa composed of a catalytic (37 kDa) and a modulator (31 kDa) subunit.
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