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Kinetics of Carboxylmethylation of the Charge Isoforms of Myelin Basic Protein by Protein Methyltransferase II

dc.contributor.authorCaamaño, Claudio A.en_US
dc.contributor.authorAzcurra, Julio M.en_US
dc.contributor.authorSellinger, Otto Z.en_US
dc.contributor.authorZand, Roberten_US
dc.date.accessioned2010-04-01T15:20:48Z
dc.date.available2010-04-01T15:20:48Z
dc.date.issued1989-12en_US
dc.identifier.citationCaamaÑo, Claudio A.; Azcurra, Julio M.; Sellinger, Otto Z.; Zand, Robert (1989). "Kinetics of Carboxylmethylation of the Charge Isoforms of Myelin Basic Protein by Protein Methyltransferase II." Journal of Neurochemistry 53(6): 1883-1888. <http://hdl.handle.net/2027.42/65821>en_US
dc.identifier.issn0022-3042en_US
dc.identifier.issn1471-4159en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/65821
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2478665&dopt=citationen_US
dc.description.abstractThe charge isoforms (C1-C5) of bovine myelin basic protein (MBP) were used as substrates for the rat brain enzyme protein carboxylmethyltransferase (PM II). The objective of these experiments was to ascertain whether the kinetic behavior of the MBP isoforms reflected differences in the structures of this molecular family. Initial velocity plots as a function of the MBP-isoform concentration showed significnt differences ( p > 0.05) among the assayed isoforms except for isoforms C2 and C4. Under the conditions of our experiment all the curves exhibited a consistent sigmoidicity. The kinetic data were best fitted by a model, previously described for the enzyme D-Β-hydroxybutyrate dehydrogenase, in which two independent sites must be randomly occupied before any catalytic activity can occur. This mechanism is substantially different from that proposed by other investigators for similar PM II enzymes and other substrates. The differences in the rates of isoform carboxylmethylation are largely accounted for by the different apparent dissociation constants K s and is explained on the basis of inherent structural differences among the charge isoforms.en_US
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dc.format.extent3110 bytes
dc.format.mimetypeapplication/pdf
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dc.publisherBlackwell Publishing Ltden_US
dc.rights1989 International Society for Neurochemistryen_US
dc.subject.otherCarboxylmethylationen_US
dc.subject.otherMyelin Basic Proteinen_US
dc.subject.otherCharge Isoformsen_US
dc.subject.otherKineticsen_US
dc.subject.otherStructureen_US
dc.titleKinetics of Carboxylmethylation of the Charge Isoforms of Myelin Basic Protein by Protein Methyltransferase IIen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNeurosciencesen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division and Department of Biological Chemistry, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationum* Mental Health Research Institute, University of Michigan, Ann Arbor, Michigan, USAen_US
dc.identifier.pmid2478665en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/65821/1/j.1471-4159.1989.tb09257.x.pdf
dc.identifier.doi10.1111/j.1471-4159.1989.tb09257.xen_US
dc.identifier.sourceJournal of Neurochemistryen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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