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Structure of human serum cholinesterase

dc.contributor.authorLockridge, Oksanaen_US
dc.date.accessioned2007-04-06T18:36:36Z
dc.date.available2007-04-06T18:36:36Z
dc.date.issued1988-10en_US
dc.identifier.citationLockridge, Oksana (1988)."Structure of human serum cholinesterase." BioEssays 9(4): 125-128. <http://hdl.handle.net/2027.42/50189>en_US
dc.identifier.issn0265-9247en_US
dc.identifier.issn1521-1878en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/50189
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3067729&dopt=citationen_US
dc.description.abstractHuman cholinesterase has recently been sequenced and cloned. It is a glycoprotein of 4 identical subunits, each subunit containing 9 carbohydrate chains and 3.5 disulfide bonds. Protein folding is likely to be very similar in human cholinesterase and Torpedo acetylcholinesterase. The cholinesterases have no significant sequence homology with the serine proteases and seem to belong to a separate serine esterase family.en_US
dc.format.extent480910 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherLife and Medical Sciencesen_US
dc.subject.otherCell & Developmental Biologyen_US
dc.titleStructure of human serum cholinesteraseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumPharmacology Department, Medical Science I, M6322, University of Michigan, Ann. Arbor, MI 48109-0626, USAen_US
dc.identifier.pmid3067729en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/50189/1/950090406_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/bies.950090406en_US
dc.identifier.sourceBioEssaysen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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