{"title":"[大鼠脑Na+,K+- atp酶催化亚基异构体对过氧化膜修饰的敏感性]。","authors":"A A Kaplia","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The comparative study of the sensitivity of Na+, K(+)-ATPase isozymes from cerebral cortex to ascorbate-dependent membrane peroxidation was conducted. With highly inactivated Na+, K(+)-ATPase the degree of inactivation of the SH-dependent ouabain-sensitive forms alpha+ (alpha 2 and alpha 3) is higher than glycoside-resistant isoform alpha 1. The process is accompanied by simultaneous lipid peroxidation and decrease of SH-groups amount in enzyme preparations. The combined nature of the oxidative Na+, K(+)-ATPase inactivation, accompanied by the direct oxidation of enzyme SH-groups and modification of lipid environment is supposed.</p>","PeriodicalId":76775,"journal":{"name":"Ukrainskii biokhimicheskii zhurnal (1978)","volume":"70 4","pages":"118-22"},"PeriodicalIF":0.0000,"publicationDate":"1998-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[The sensitivity of catalytic subunit isoforms of Na+,K+-ATPase of rat brain to peroxide membrane modification].\",\"authors\":\"A A Kaplia\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The comparative study of the sensitivity of Na+, K(+)-ATPase isozymes from cerebral cortex to ascorbate-dependent membrane peroxidation was conducted. With highly inactivated Na+, K(+)-ATPase the degree of inactivation of the SH-dependent ouabain-sensitive forms alpha+ (alpha 2 and alpha 3) is higher than glycoside-resistant isoform alpha 1. The process is accompanied by simultaneous lipid peroxidation and decrease of SH-groups amount in enzyme preparations. The combined nature of the oxidative Na+, K(+)-ATPase inactivation, accompanied by the direct oxidation of enzyme SH-groups and modification of lipid environment is supposed.</p>\",\"PeriodicalId\":76775,\"journal\":{\"name\":\"Ukrainskii biokhimicheskii zhurnal (1978)\",\"volume\":\"70 4\",\"pages\":\"118-22\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ukrainskii biokhimicheskii zhurnal (1978)\",\"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":"Ukrainskii biokhimicheskii zhurnal (1978)","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[The sensitivity of catalytic subunit isoforms of Na+,K+-ATPase of rat brain to peroxide membrane modification].
The comparative study of the sensitivity of Na+, K(+)-ATPase isozymes from cerebral cortex to ascorbate-dependent membrane peroxidation was conducted. With highly inactivated Na+, K(+)-ATPase the degree of inactivation of the SH-dependent ouabain-sensitive forms alpha+ (alpha 2 and alpha 3) is higher than glycoside-resistant isoform alpha 1. The process is accompanied by simultaneous lipid peroxidation and decrease of SH-groups amount in enzyme preparations. The combined nature of the oxidative Na+, K(+)-ATPase inactivation, accompanied by the direct oxidation of enzyme SH-groups and modification of lipid environment is supposed.