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Mammalian tyrosinase: Effect of ions on enzyme action

dc.contributor.authorLerner, Aaron Bunsenen_US
dc.date.accessioned2006-04-13T15:05:26Z
dc.date.available2006-04-13T15:05:26Z
dc.date.issued1952-04en_US
dc.identifier.citationLerner, Aaron Bunsen (1952/04)."Mammalian tyrosinase: Effect of ions on enzyme action." Archives of Biochemistry and Biophysics 36(2): 473-481. <http://hdl.handle.net/2027.42/32541>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DW3FN7-1R5/2/966b5a58486a5ad14dbcce6343e15be0en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32541
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14944275&dopt=citationen_US
dc.description.abstract1. 1. The univalent cations Li+, Na+, K+, and NH4+ have no effect on tyrosinase action.2. 2. The anions, fluoride, chloride, acetate, and oxalate, consistently inhibit the tyrosine-tyrosinase and dopa-tyrosinase reactions. Iodate, persulfate, and nitrite also inhibit these reactions. Relatively large amounts of these anions are required to produce inhibition.3. 3. Of 24 metal ions tested, only mercury, silver, and gold can produce an inactive enzyme preparation. The ions compete with copper ions for active centers on apotyrosinase. These competitive inhibition reactions are only slowly reversible.4. 4. No cations or anions accelerate tyrosinase action.5. 5. Copper ions are not bound to tyrosinase by a mercaptide linkage.en_US
dc.format.extent440842 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleMammalian tyrosinase: Effect of ions on enzyme actionen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Dermatology, University of Michigan School of Medicine, Ann Arbor, Michigan, USAen_US
dc.identifier.pmid14944275en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32541/1/0000652.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(52)90435-9en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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