{"title":"[关于结合下丘脑冠状动脉扩张物质的心脏蛋白的新发现]。","authors":"R M Srapionian, S S Misirian, A A Galoian","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>We had previously shown that the protein component obtained from heart muscle by 0.1--0.2 saturation with ammonium sulfate exhibits a coronarodilatatory effect. Later on we succeeded in isolating from this protein complex, through dialysis, two coronaoractive low molecular compounds, one of which is apparently a neurohormone. In the present study we isolated, purified and studied the features of this protein complex. The results of gel filtration on Sephadex G-100 confirmed the presence of two different coronaroactive neurohormone binding proteins in heart muscle. The active fractions have been also purified through ion exchange chromatography on diethylaminoethyl cellulose. The purity of these fractions was tested through electrophoresis on 7.5% polyacrylamide gel. In the last stage of purification the active proteins moved towards the anode by one zone.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"122-8"},"PeriodicalIF":0.0000,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[New findings concerning cardiac proteins binding the coronary dilating substances of the hypothalamus].\",\"authors\":\"R M Srapionian, S S Misirian, A A Galoian\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>We had previously shown that the protein component obtained from heart muscle by 0.1--0.2 saturation with ammonium sulfate exhibits a coronarodilatatory effect. Later on we succeeded in isolating from this protein complex, through dialysis, two coronaoractive low molecular compounds, one of which is apparently a neurohormone. In the present study we isolated, purified and studied the features of this protein complex. The results of gel filtration on Sephadex G-100 confirmed the presence of two different coronaroactive neurohormone binding proteins in heart muscle. The active fractions have been also purified through ion exchange chromatography on diethylaminoethyl cellulose. The purity of these fractions was tested through electrophoresis on 7.5% polyacrylamide gel. In the last stage of purification the active proteins moved towards the anode by one zone.</p>\",\"PeriodicalId\":76813,\"journal\":{\"name\":\"Voprosy biokhimii mozga\",\"volume\":\"10 \",\"pages\":\"122-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1975-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Voprosy biokhimii mozga\",\"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":"Voprosy biokhimii mozga","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[New findings concerning cardiac proteins binding the coronary dilating substances of the hypothalamus].
We had previously shown that the protein component obtained from heart muscle by 0.1--0.2 saturation with ammonium sulfate exhibits a coronarodilatatory effect. Later on we succeeded in isolating from this protein complex, through dialysis, two coronaoractive low molecular compounds, one of which is apparently a neurohormone. In the present study we isolated, purified and studied the features of this protein complex. The results of gel filtration on Sephadex G-100 confirmed the presence of two different coronaroactive neurohormone binding proteins in heart muscle. The active fractions have been also purified through ion exchange chromatography on diethylaminoethyl cellulose. The purity of these fractions was tested through electrophoresis on 7.5% polyacrylamide gel. In the last stage of purification the active proteins moved towards the anode by one zone.