{"title":"荞麦籽豆素富含赖氨酸和蛋氨酸的基本亚基：结构研究的一些结果。","authors":"M K Rout, N K Chrungoo","doi":"10.1080/15216549900202033","DOIUrl":null,"url":null,"abstract":"<p><p>The 26 kD basic subunit of 280 kD buckwheat grain legumin has been partially characterized by measurement of its fluorescence and CD spectra. The protein has 22% alpha-helix, 36% beta-sheet, 12% beta-turn and 30% random coil secondary structure. In comparison with the basic subunits of other legumin-type proteins, the buckwheat legumin subunit has a high content of lysine and methionine. The protein also has higher ratios of lysine to arginine and methionine to arginine.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 6","pages":"921-6"},"PeriodicalIF":0.0000,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900202033","citationCount":"13","resultStr":"{\"title\":\"The lysine and methionine rich basic subunit of buckwheat grain legumin: some results of a structural study.\",\"authors\":\"M K Rout, N K Chrungoo\",\"doi\":\"10.1080/15216549900202033\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The 26 kD basic subunit of 280 kD buckwheat grain legumin has been partially characterized by measurement of its fluorescence and CD spectra. The protein has 22% alpha-helix, 36% beta-sheet, 12% beta-turn and 30% random coil secondary structure. In comparison with the basic subunits of other legumin-type proteins, the buckwheat legumin subunit has a high content of lysine and methionine. The protein also has higher ratios of lysine to arginine and methionine to arginine.</p>\",\"PeriodicalId\":8770,\"journal\":{\"name\":\"Biochemistry and molecular biology international\",\"volume\":\"47 6\",\"pages\":\"921-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1999-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/15216549900202033\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry and molecular biology international\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/15216549900202033\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry and molecular biology international","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/15216549900202033","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The lysine and methionine rich basic subunit of buckwheat grain legumin: some results of a structural study.
The 26 kD basic subunit of 280 kD buckwheat grain legumin has been partially characterized by measurement of its fluorescence and CD spectra. The protein has 22% alpha-helix, 36% beta-sheet, 12% beta-turn and 30% random coil secondary structure. In comparison with the basic subunits of other legumin-type proteins, the buckwheat legumin subunit has a high content of lysine and methionine. The protein also has higher ratios of lysine to arginine and methionine to arginine.
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