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• W83848988 abstract "Research Article1 August 1995free access Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer. P. Klatt P. Klatt Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author K. Schmidt K. Schmidt Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author D. Lehner D. Lehner Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author O. Glatter O. Glatter Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author H. P. Bächinger H. P. Bächinger Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author B. Mayer B. Mayer Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author P. Klatt P. Klatt Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author K. Schmidt K. Schmidt Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author D. Lehner D. Lehner Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author O. Glatter O. Glatter Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author H. P. Bächinger H. P. Bächinger Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author B. Mayer B. Mayer Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. Search for more papers by this author Author Information P. Klatt1, K. Schmidt1, D. Lehner1, O. Glatter1, H. P. Bächinger1 and B. Mayer1 1Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. The EMBO Journal (1995)14:3687-3695https://doi.org/10.1002/j.1460-2075.1995.tb00038.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Nitric oxide synthases (NOSs), which catalyze the formation of the ubiquitous biological messenger molecule nitric oxide, represent unique cytochrome P-450s, containing reductase and mono-oxygenase domains within one polypeptide and requiring tetrahydrobiopterin as cofactor. To investigate whether tetrahydrobiopterin functions as an allosteric effector of NOS, we have analyzed the effect of the pteridine on the conformation of neuronal NOS purified from porcine brain by means of circular dichroism, velocity sedimentation, dynamic light scattering and SDS-polyacrylamide gel electrophoresis. We report for the first time the secondary structure of NOS, showing that the neuronal isozyme contains 30% alpha-helix, 14% antiparallel beta-sheet, 7% parallel beta-sheet, 19% turns and 31% other structures. The secondary structure of neuronal NOS was neither modulated nor stabilized by tetrahydrobiopterin, and the pteridine did not affect the quaternary structure of the protein, which appears to be an elongated homodimer with an axial ratio of approximately 20/1 under native conditions. Low temperature SDS-polyacrylamide gel electrophoresis revealed that tetrahydrobiopterin and L-arginine synergistically convert neuronal NOS into an exceptionally stable, non-covalently linked homodimer surviving in 2% SDS and 5% 2-mercaptoethanol. Ligand-induced formation of an SDS-resistant dimer is unprecedented and suggests a novel role for tetrahydrobiopterin and L-arginine in the allosteric regulation of protein subunit interactions. Previous ArticleNext Article Volume 14Issue 151 August 1995In this issue RelatedDetailsLoading ..." @default.
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• W83848988 date "1995-08-01" @default.
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• W83848988 title "Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer." @default.
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• W83848988 doi "https://doi.org/10.1002/j.1460-2075.1995.tb00038.x" @default.
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