Inactivation of macrophage nitric oxide synthase activity by NG-Methyl-L-arginine
dc.contributor.author | Olken, Norman M. | en_US |
dc.contributor.author | Rusche, Kristin M. | en_US |
dc.contributor.author | Richards, Michael K. | en_US |
dc.contributor.author | Marletta, Michael A. | en_US |
dc.date.accessioned | 2006-04-10T14:41:31Z | |
dc.date.available | 2006-04-10T14:41:31Z | |
dc.date.issued | 1991-06-14 | en_US |
dc.identifier.citation | Olken, Norman M., Rusche, Kristin M., Richards, Michael K., Marletta, Michael A. (1991/06/14)."Inactivation of macrophage nitric oxide synthase activity by NG-Methyl-L-arginine." Biochemical and Biophysical Research Communications 177(2): 828-833. <http://hdl.handle.net/2027.42/29284> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4DXRY44-179/2/57345ce5dc2e048716c38599a8c38c93 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29284 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2049105&dopt=citation | en_US |
dc.description.abstract | [middle dot]N=O synthase catalyzes the oxidation of one of the two chemically equivalent guanido nitrogens of L-arginine to nitric oxide ([middle dot]N=O). NG-Methyl-L-arginine has been previously characterized as a potent competitive inhibitor of both major types of [middle dot]N=O synthases. Initial rate kinetics were performed with a spectrophotometric assay based on the oxidation of oxy- to methemoglobin by [middle dot]N=O. NG-Methyl-L-arginine was a competitive inhibitor of [middle dot]N=O synthase activity derived from activated murine macrophages with a Ki of 6.2 [mu]M. When the enzyme was pre-incubated in the presence of the required cofactors NADPH and tetrahydrobiopterin, time- and concentration-dependent irreversible inactivation of the activity was observed. At 37[deg] C the kinact was 0.050 min-1. This inactivation process exhibited substrate protection, saturation kinetics and required the cofactors necessary for enzymatic turnover. These data indicate that NG-methyl-L-arginine asts as a mechanism-based enzyme inactivator of murine macrophage [middle dot]N=O synthase. | en_US |
dc.format.extent | 486217 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Inactivation of macrophage nitric oxide synthase activity by NG-Methyl-L-arginine | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy University of Michigan, Ann Arbor, MI 48109-1065, USA | en_US |
dc.contributor.affiliationum | the Department of Biological Chemistry, School of Medicine, University of Michigan, Ann Arbor, MI 48109-1065, USA | en_US |
dc.contributor.affiliationum | the Department of Biological Chemistry, School of Medicine, University of Michigan, Ann Arbor, MI 48109-1065, USA | en_US |
dc.contributor.affiliationum | Interdepartmental Program in Medicinal Chemistry, College of Pharmacy University of Michigan, Ann Arbor, MI 48109-1065, USA;the Department of Biological Chemistry, School of Medicine, University of Michigan, Ann Arbor, MI 48109-1065, USA | en_US |
dc.identifier.pmid | 2049105 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29284/1/0000343.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-291X(91)91864-9 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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