{"title":"F抗原。2化学和物理性质。","authors":"R. Utzinger","doi":"10.1159/000162716","DOIUrl":null,"url":null,"abstract":"Physical and chemical properties of the liver-specific F antigen suggested a model for the labile quarternary structure of the protein. The native molecule showed a size slightly larger than 60,000 dalton (d), which was reduced to about 40,000 d under acidic conditions. Breaking of hydrogen bonds by chaotropic treatment resulted in the release of components of 30,000, 7,000 and 2,000 d. The smallest component was split to fragments of about 1,000 d by the reducing action of sulfhydryl compounds.","PeriodicalId":19854,"journal":{"name":"Pathologia et microbiologia","volume":"12 1","pages":"3-14"},"PeriodicalIF":0.0000,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"F antigen. II. Chemical and physical properties.\",\"authors\":\"R. Utzinger\",\"doi\":\"10.1159/000162716\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Physical and chemical properties of the liver-specific F antigen suggested a model for the labile quarternary structure of the protein. The native molecule showed a size slightly larger than 60,000 dalton (d), which was reduced to about 40,000 d under acidic conditions. Breaking of hydrogen bonds by chaotropic treatment resulted in the release of components of 30,000, 7,000 and 2,000 d. The smallest component was split to fragments of about 1,000 d by the reducing action of sulfhydryl compounds.\",\"PeriodicalId\":19854,\"journal\":{\"name\":\"Pathologia et microbiologia\",\"volume\":\"12 1\",\"pages\":\"3-14\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1975-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Pathologia et microbiologia\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000162716\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Pathologia et microbiologia","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000162716","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Physical and chemical properties of the liver-specific F antigen suggested a model for the labile quarternary structure of the protein. The native molecule showed a size slightly larger than 60,000 dalton (d), which was reduced to about 40,000 d under acidic conditions. Breaking of hydrogen bonds by chaotropic treatment resulted in the release of components of 30,000, 7,000 and 2,000 d. The smallest component was split to fragments of about 1,000 d by the reducing action of sulfhydryl compounds.
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