{"title":"PDI, PPI和伴侣催化重组人IL-2和GM-CSF的再折叠。","authors":"M. Xu, W. Meng, X. Ma","doi":"10.1360/YB1995-38-4-429","DOIUrl":null,"url":null,"abstract":"The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers. PPI can increase the rate of folding reaction while chaperone can prevent the aggregation during the folding process. In addition, there is a synergistic effect between them.","PeriodicalId":21648,"journal":{"name":"Science in China. Series B, Chemistry, life sciences & earth sciences","volume":"256 1","pages":"429-37"},"PeriodicalIF":0.0000,"publicationDate":"1995-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF.\",\"authors\":\"M. Xu, W. Meng, X. Ma\",\"doi\":\"10.1360/YB1995-38-4-429\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers. PPI can increase the rate of folding reaction while chaperone can prevent the aggregation during the folding process. In addition, there is a synergistic effect between them.\",\"PeriodicalId\":21648,\"journal\":{\"name\":\"Science in China. Series B, Chemistry, life sciences & earth sciences\",\"volume\":\"256 1\",\"pages\":\"429-37\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-04-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Science in China. Series B, Chemistry, life sciences & earth sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1360/YB1995-38-4-429\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science in China. Series B, Chemistry, life sciences & earth sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1360/YB1995-38-4-429","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF.
The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers. PPI can increase the rate of folding reaction while chaperone can prevent the aggregation during the folding process. In addition, there is a synergistic effect between them.
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