{"title":"重组人神经激肽-1受体在昆虫细胞中的表达与溶解。","authors":"K E Mazina, C D Strader, T M Fong","doi":"10.3109/10799899409066997","DOIUrl":null,"url":null,"abstract":"<p><p>The human neurokinin-1 receptor has been expressed in insect cells using a recombinant baculovirus. The expression level is about 10 times higher than that obtained in mammalian cells. The recombinant receptor was solubilized with CHAPS, and a PEG precipitation procedure was shown to be effective in regaining high affinity substance P binding. This system should allow large scale purification of the human neurokinin-1 receptor.</p>","PeriodicalId":16948,"journal":{"name":"Journal of receptor research","volume":"14 1","pages":"63-73"},"PeriodicalIF":0.0000,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10799899409066997","citationCount":"18","resultStr":"{\"title\":\"Expression and solubilization of a recombinant human neurokinin-1 receptor in insect cells.\",\"authors\":\"K E Mazina, C D Strader, T M Fong\",\"doi\":\"10.3109/10799899409066997\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The human neurokinin-1 receptor has been expressed in insect cells using a recombinant baculovirus. The expression level is about 10 times higher than that obtained in mammalian cells. The recombinant receptor was solubilized with CHAPS, and a PEG precipitation procedure was shown to be effective in regaining high affinity substance P binding. This system should allow large scale purification of the human neurokinin-1 receptor.</p>\",\"PeriodicalId\":16948,\"journal\":{\"name\":\"Journal of receptor research\",\"volume\":\"14 1\",\"pages\":\"63-73\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.3109/10799899409066997\",\"citationCount\":\"18\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of receptor research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3109/10799899409066997\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of receptor research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/10799899409066997","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Expression and solubilization of a recombinant human neurokinin-1 receptor in insect cells.
The human neurokinin-1 receptor has been expressed in insect cells using a recombinant baculovirus. The expression level is about 10 times higher than that obtained in mammalian cells. The recombinant receptor was solubilized with CHAPS, and a PEG precipitation procedure was shown to be effective in regaining high affinity substance P binding. This system should allow large scale purification of the human neurokinin-1 receptor.
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