{"title":"Genetic locus, primary structure, and chemical synthesis of human immunodeficiency virys protease","authors":"Terry D. Copeland , Stephen Oroszlan","doi":"10.1016/0735-0651(88)90010-6","DOIUrl":null,"url":null,"abstract":"<div><p>The genetic locus and primary structure of the human immunodeficiency virus (HIV) protease was determined by comparing the data of protein analyses with the published data of the gene analysis. The complete sequence of HIV-1 and HIV-2 protease was synthesized by solid-phase peptide synthesis. The synthetic protease was capable of accurately cleaving synthetic peptide substrates corresponding to known cleavage sites in <em>gag</em> polyproteins of HIV-1, HIV-2, and murine leukemia virus. The chemical synthesis of protease confirms the DNA sequence and provides a means of rapidly producing active protease in substantial quantities for biochemical and physical studies.</p></div>","PeriodicalId":77714,"journal":{"name":"Gene analysis techniques","volume":"5 6","pages":"Pages 109-115"},"PeriodicalIF":0.0000,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0735-0651(88)90010-6","citationCount":"64","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Gene analysis techniques","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0735065188900106","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 64
Abstract
The genetic locus and primary structure of the human immunodeficiency virus (HIV) protease was determined by comparing the data of protein analyses with the published data of the gene analysis. The complete sequence of HIV-1 and HIV-2 protease was synthesized by solid-phase peptide synthesis. The synthetic protease was capable of accurately cleaving synthetic peptide substrates corresponding to known cleavage sites in gag polyproteins of HIV-1, HIV-2, and murine leukemia virus. The chemical synthesis of protease confirms the DNA sequence and provides a means of rapidly producing active protease in substantial quantities for biochemical and physical studies.