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Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification

dc.contributor.authorChegwidden, W. Richarden_US
dc.contributor.authorTashian, Richard E.en_US
dc.contributor.authorChristiansen, Eriken_US
dc.contributor.authorJohansen, Jack T.en_US
dc.date.accessioned2006-09-11T14:25:00Z
dc.date.available2006-09-11T14:25:00Z
dc.date.issued1984-07en_US
dc.identifier.citationTashian, Richard E.; Johansen, Jack T.; Christiansen, Erik; Chegwidden, W. Richard; (1984). "Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification." Bioscience Reports 4(7): 573-579. <http://hdl.handle.net/2027.42/44191>en_US
dc.identifier.issn0144-8463en_US
dc.identifier.issn1573-4935en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/44191
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6433999&dopt=citationen_US
dc.description.abstractPurified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.en_US
dc.format.extent400381 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers; The Biochemical Society ; Springer Science+Business Mediaen_US
dc.subject.otherBiochemistry, Generalen_US
dc.subject.otherLife Sciencesen_US
dc.subject.otherAnimal Biochemistryen_US
dc.subject.otherPlant Sciencesen_US
dc.subject.otherAnimal Anatomy / Morphology / Histologyen_US
dc.titleActivation of mammalian skeletal-muscle carbonic anhydrase III by arginine modificationen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelGeneticsen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, Carlsberg Laboratory, DK-2500, Copenhagen Valby, Denmark; Department of Human Genetics, University of Michigan Medical School, 1137 E. Catherine St., 48109, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationotherDepartment of Chemistry, Carlsberg Laboratory, DK-2500, Copenhagen Valby, Denmark; Carlsberg Biotechnology Ltd. A/S, DK-2200, Copenhagen N, Denmarken_US
dc.contributor.affiliationotherClinical Chemistry Laboratory, Kommunehospitalet, DK-1399, Copenhagen K, Denmarken_US
dc.contributor.affiliationotherDepartment of Biological Sciences, Sheffield City Polytechnic, S1 1WB, Sheffield, UKen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid6433999en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/44191/1/10540_2005_Article_BF01121914.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1007/BF01121914en_US
dc.identifier.sourceBioscience Reportsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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