{"title":"蛋白酶对赖氨酸氨基的区域选择性修饰。","authors":"H. Kitaguchi, M. Ono, I. Itoh, A. Klibanov","doi":"10.1080/00021369.1991.10857914","DOIUrl":null,"url":null,"abstract":"The regioselectivity of six serine proteases for the amino groups of lysine was investigated. alpha-Chymotrypsin showed a preference for the alpha-amino group, although the selectivity can be varied 10-fold depending on the reaction medium. Subtilisin Carlsberg and other bacterial proteases were highly specific for the epsilon-amino group, regardless of the reaction medium: they were used as catalysts for the preparative synthesis of isopeptides in anhydrous tert-amyl alcohol.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"26 1","pages":"3067-73"},"PeriodicalIF":0.0000,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":"{\"title\":\"Regioselective modification of Lysine's amino groups by proteases.\",\"authors\":\"H. Kitaguchi, M. Ono, I. Itoh, A. Klibanov\",\"doi\":\"10.1080/00021369.1991.10857914\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The regioselectivity of six serine proteases for the amino groups of lysine was investigated. alpha-Chymotrypsin showed a preference for the alpha-amino group, although the selectivity can be varied 10-fold depending on the reaction medium. Subtilisin Carlsberg and other bacterial proteases were highly specific for the epsilon-amino group, regardless of the reaction medium: they were used as catalysts for the preparative synthesis of isopeptides in anhydrous tert-amyl alcohol.\",\"PeriodicalId\":7729,\"journal\":{\"name\":\"Agricultural and biological chemistry\",\"volume\":\"26 1\",\"pages\":\"3067-73\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Agricultural and biological chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/00021369.1991.10857914\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Agricultural and biological chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/00021369.1991.10857914","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Regioselective modification of Lysine's amino groups by proteases.
The regioselectivity of six serine proteases for the amino groups of lysine was investigated. alpha-Chymotrypsin showed a preference for the alpha-amino group, although the selectivity can be varied 10-fold depending on the reaction medium. Subtilisin Carlsberg and other bacterial proteases were highly specific for the epsilon-amino group, regardless of the reaction medium: they were used as catalysts for the preparative synthesis of isopeptides in anhydrous tert-amyl alcohol.
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