{"title":"小鼠骨骼肌中性核糖核酸酶II和核糖核酸酶II抑制剂复合物的异质性","authors":"B.W. Little, L.S. Whittingham","doi":"10.1016/0005-2787(81)90015-0","DOIUrl":null,"url":null,"abstract":"<div><p>Using either DEAE-cellulose chromatography or pH 4–6 isoelectric focusing, we have separated mouse skeletal muscle neutral RNAase II-inhibitor complex into two fractions (designated α and β).<em>para</em>-Hydroxymercuriphenylsulfonate-induced dissociation/inactivation of the inhibitor yields free RNAase II enzyme fractions with differing pH profiles, CM-cellulose chromatographic behavior and reactivity with the RNAase II inhibitor of human placenta. However, the free RNAase fractions react equally with purified inhibitor from skeletal muscle and are not separable by pH 8–9.5 isoelectric focusing. These data suggest that mouse skeletal muscle has two heterogeneous forms of RNAase II. Additionally, heterologous RNAase II inhibitors may be used as investigational tools when probing neutral RNAase II heterogeneity.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 2","pages":"Pages 251-255"},"PeriodicalIF":0.0000,"publicationDate":"1981-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90015-0","citationCount":"5","resultStr":"{\"title\":\"Heterogeneity of neutral ribonuclease II and ribonuclease II-inhibitor complex from mouse skeletal muscle\",\"authors\":\"B.W. Little, L.S. Whittingham\",\"doi\":\"10.1016/0005-2787(81)90015-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Using either DEAE-cellulose chromatography or pH 4–6 isoelectric focusing, we have separated mouse skeletal muscle neutral RNAase II-inhibitor complex into two fractions (designated α and β).<em>para</em>-Hydroxymercuriphenylsulfonate-induced dissociation/inactivation of the inhibitor yields free RNAase II enzyme fractions with differing pH profiles, CM-cellulose chromatographic behavior and reactivity with the RNAase II inhibitor of human placenta. However, the free RNAase fractions react equally with purified inhibitor from skeletal muscle and are not separable by pH 8–9.5 isoelectric focusing. These data suggest that mouse skeletal muscle has two heterogeneous forms of RNAase II. Additionally, heterologous RNAase II inhibitors may be used as investigational tools when probing neutral RNAase II heterogeneity.</p></div>\",\"PeriodicalId\":100164,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis\",\"volume\":\"655 2\",\"pages\":\"Pages 251-255\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-09-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2787(81)90015-0\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005278781900150\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005278781900150","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Heterogeneity of neutral ribonuclease II and ribonuclease II-inhibitor complex from mouse skeletal muscle
Using either DEAE-cellulose chromatography or pH 4–6 isoelectric focusing, we have separated mouse skeletal muscle neutral RNAase II-inhibitor complex into two fractions (designated α and β).para-Hydroxymercuriphenylsulfonate-induced dissociation/inactivation of the inhibitor yields free RNAase II enzyme fractions with differing pH profiles, CM-cellulose chromatographic behavior and reactivity with the RNAase II inhibitor of human placenta. However, the free RNAase fractions react equally with purified inhibitor from skeletal muscle and are not separable by pH 8–9.5 isoelectric focusing. These data suggest that mouse skeletal muscle has two heterogeneous forms of RNAase II. Additionally, heterologous RNAase II inhibitors may be used as investigational tools when probing neutral RNAase II heterogeneity.
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