{"title":"cutirubrum盐杆菌热转变的量热研究。","authors":"K C Cho, K C Chow, K K Mark","doi":"10.1139/o82-049","DOIUrl":null,"url":null,"abstract":"<p><p>The thermal transitions of Halobacterium cutirubrum have been examined by differential scanning calorimetry. Two distinct peaks corresponding to the denaturation of two major protein components were observed in the heating curves. One of the peaks has been assigned to the denaturation of the envelope glycoprotein. The variations of the denaturation temperatures with the addition of glucose, glycerol, NaNO3, and NaSCN are consistent with the previous proposal that hydrophobic interactions are essential in stabilizing the glycoprotein.</p>","PeriodicalId":9508,"journal":{"name":"Canadian journal of biochemistry","volume":" ","pages":"419-21"},"PeriodicalIF":0.0000,"publicationDate":"1982-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1139/o82-049","citationCount":"4","resultStr":"{\"title\":\"A calorimetric study of the thermal transitions of Halobacterium cutirubrum.\",\"authors\":\"K C Cho, K C Chow, K K Mark\",\"doi\":\"10.1139/o82-049\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The thermal transitions of Halobacterium cutirubrum have been examined by differential scanning calorimetry. Two distinct peaks corresponding to the denaturation of two major protein components were observed in the heating curves. One of the peaks has been assigned to the denaturation of the envelope glycoprotein. The variations of the denaturation temperatures with the addition of glucose, glycerol, NaNO3, and NaSCN are consistent with the previous proposal that hydrophobic interactions are essential in stabilizing the glycoprotein.</p>\",\"PeriodicalId\":9508,\"journal\":{\"name\":\"Canadian journal of biochemistry\",\"volume\":\" \",\"pages\":\"419-21\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1982-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1139/o82-049\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Canadian journal of biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1139/o82-049\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Canadian journal of biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1139/o82-049","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A calorimetric study of the thermal transitions of Halobacterium cutirubrum.
The thermal transitions of Halobacterium cutirubrum have been examined by differential scanning calorimetry. Two distinct peaks corresponding to the denaturation of two major protein components were observed in the heating curves. One of the peaks has been assigned to the denaturation of the envelope glycoprotein. The variations of the denaturation temperatures with the addition of glucose, glycerol, NaNO3, and NaSCN are consistent with the previous proposal that hydrophobic interactions are essential in stabilizing the glycoprotein.
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