{"title":"12型化脓性链球菌M蛋白。电聚焦分离和一些分子量依赖性质。","authors":"J Havlícek","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A method for the isolation and purification of M protein was developed. Purified cell walls were sonically disrupted, solubilized M protein was precipitated by ammonium sulphate and then electrofocused. Both in this material and in hot acid extracts type-specific trypsin-sensitive antigens with two separately precipitating moieties were found. Evidence is adduced showing that they both belong to the M protein complex. The molecular weight of our purified M protein ranged between 400,000 and 20,000 daltons, giving a peak at 150,000 daltons. The pI of this material was found to be 5.4-5.6. There were marked differences between the behaviour of the low, medium and high molecular weight fractions obtained from purified M protein by gel filtration.</p>","PeriodicalId":19854,"journal":{"name":"Pathologia et microbiologia","volume":"42 3","pages":"147-58"},"PeriodicalIF":0.0000,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"M protein of type 12 Strepto coccus pyogenes. Isolation by electrofocusing and some molecular weight-dependent properties.\",\"authors\":\"J Havlícek\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A method for the isolation and purification of M protein was developed. Purified cell walls were sonically disrupted, solubilized M protein was precipitated by ammonium sulphate and then electrofocused. Both in this material and in hot acid extracts type-specific trypsin-sensitive antigens with two separately precipitating moieties were found. Evidence is adduced showing that they both belong to the M protein complex. The molecular weight of our purified M protein ranged between 400,000 and 20,000 daltons, giving a peak at 150,000 daltons. The pI of this material was found to be 5.4-5.6. There were marked differences between the behaviour of the low, medium and high molecular weight fractions obtained from purified M protein by gel filtration.</p>\",\"PeriodicalId\":19854,\"journal\":{\"name\":\"Pathologia et microbiologia\",\"volume\":\"42 3\",\"pages\":\"147-58\"},\"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\":\"\",\"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":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
M protein of type 12 Strepto coccus pyogenes. Isolation by electrofocusing and some molecular weight-dependent properties.
A method for the isolation and purification of M protein was developed. Purified cell walls were sonically disrupted, solubilized M protein was precipitated by ammonium sulphate and then electrofocused. Both in this material and in hot acid extracts type-specific trypsin-sensitive antigens with two separately precipitating moieties were found. Evidence is adduced showing that they both belong to the M protein complex. The molecular weight of our purified M protein ranged between 400,000 and 20,000 daltons, giving a peak at 150,000 daltons. The pI of this material was found to be 5.4-5.6. There were marked differences between the behaviour of the low, medium and high molecular weight fractions obtained from purified M protein by gel filtration.
分享
京公网安备 11010802042870号
京ICP备2023020795号-1
求助内容：
应助结果提醒方式：
扫码关注我们
