{"title":"Consequences of exposure of rats to hyperoxygenation for actomyosin-like protein from synaptosomes of brain.","authors":"U Rafałowska, W Gordon-Majszak, Z Dabrowiecki","doi":"10.1007/BF03160126","DOIUrl":null,"url":null,"abstract":"<p><p>This paper describes the changes caused by in vivo hyperoxygenation of rats in the brain synaptosomal actomyosin-like protein preparation. We demonstrate that this preparation is composed of protein and phospholipid components attached to each other. Upon hyperoxygenation, a peroxidation of phospholipids in the lipid component proceeds. Simultaneously, with the increase of malondialdehyde, conjugated double bonds, and fluorescence intensity levels, a decrease of protein -SH groups levels, and Mg2+-dependent ATPase activity is observed. The above changes reduce the ability of the protein to superprecipitate, which reflects a contractile reaction in vivo.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"5 2","pages":"107-15"},"PeriodicalIF":0.0000,"publicationDate":"1986-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF03160126","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Neurochemical pathology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF03160126","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
This paper describes the changes caused by in vivo hyperoxygenation of rats in the brain synaptosomal actomyosin-like protein preparation. We demonstrate that this preparation is composed of protein and phospholipid components attached to each other. Upon hyperoxygenation, a peroxidation of phospholipids in the lipid component proceeds. Simultaneously, with the increase of malondialdehyde, conjugated double bonds, and fluorescence intensity levels, a decrease of protein -SH groups levels, and Mg2+-dependent ATPase activity is observed. The above changes reduce the ability of the protein to superprecipitate, which reflects a contractile reaction in vivo.