Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease
| العنوان: | Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease |
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| المؤلفون: | Christine Debouck, James E. Strickler, Thomas D. Meek, Brian D. Dayton, Brian W. Metcalf, Martin Rosenberg, Joselina G. Gorniak, Geoffrey B. Dreyer, Victoria W. Magaard, Michael L. Moore |
| المصدر: | Proceedings of the National Academy of Sciences. 86:1841-1845 |
| بيانات النشر: | Proceedings of the National Academy of Sciences, 1989. |
| سنة النشر: | 1989 |
| مصطلحات موضوعية: | TMPRSS6, Macromolecular Substances, Proteolysis, medicine.medical_treatment, Retroviridae Proteins, Gene Products, gag, Substrate Specificity, law.invention, Nitrophenols, law, Endopeptidases, Centrifugation, Density Gradient, Escherichia coli, medicine, Aspartic Acid Endopeptidases, Protease Inhibitors, chemistry.chemical_classification, Binding Sites, Multidisciplinary, Protease, medicine.diagnostic_test, biology, HIV, Active site, Hydrogen-Ion Concentration, Molecular biology, Peptide Fragments, Recombinant Proteins, Molecular Weight, NS2-3 protease, Kinetics, Enzyme, Biochemistry, chemistry, Chromatography, Gel, Recombinant DNA, biology.protein, Epoxy Compounds, Electrophoresis, Polyacrylamide Gel, Oligopeptides, MASP1, Research Article |
| الوصف: | Recombinant human immunodeficiency virus 1 (HIV-1) protease, purified from a bacterial expression system, processed a recombinant form of its natural substrate, Pr55gag, into protein fragments that possess molecular weights commensurate with those of the virion gag proteins. Molecular weights of the protease obtained under denaturing and nondenaturing conditions (11,000 and 22,000, respectively) and chemical crosslinking studies were consistent with a dimeric structure for the active enzyme. The protease appropriately cleaved the nonapeptide Ac-Arg-Ala-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2 between the tyrosine and proline residues. HIV-1 protease was sensitive to inactivators of the aspartic proteases. The aspartic protease inactivator 1,2-epoxy-3-(4-nitrophenoxy)propane produced irreversible, time-dependent inactivation of the protease. The pH-dependent kinetics of this inactivator were consistent with the requirement of an unprotonated carboxyl group in the active site of the enzyme, suggesting that HIV-1 protease is also an aspartic protease. |
| تدمد: | 1091-6490 0027-8424 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3d0e2fdf788638f51929e7091b9ba0e https://doi.org/10.1073/pnas.86.6.1841 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....c3d0e2fdf788638f51929e7091b9ba0e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10916490 00278424 |
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