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Isolation of an acid protease from rabbit reticulocytes and evidence for its role in processing redox proteins during erythroid maturation
dc.contributor.authorSchafer, Dorothy A.en_US
dc.contributor.authorHultquist, Donald E.en_US
dc.date.accessioned2006-04-07T18:04:58Z
dc.date.available2006-04-07T18:04:58Z
dc.date.issued1981-06-30en_US
dc.identifier.citationSchafer, Dorothy A., Hultquist, Donald E. (1981/06/30)."Isolation of an acid protease from rabbit reticulocytes and evidence for its role in processing redox proteins during erythroid maturation." Biochemical and Biophysical Research Communications 100(4): 1555-1561. <http://hdl.handle.net/2027.42/24341>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DYM9YK-MJ/2/95b1199de64f0e934e8254f4f4451dc5en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/24341
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7028033&dopt=citationen_US
dc.description.abstractA protease which generates a soluble hemepeptide from bovine liver microsomal cytochrome has been isolated from the membrane fraction of rabbit reticulocytes. Inhibition by pepstatin and an acidic pH optimum indicate that the protease belongs to the acid protease class. Little cytochrome -processing activity is observed in rabbit erythrocytes. We suggest that the protease may be involved in the processing which generates the proteins of the methemoglobin reduction system from their membrane-bound precursors during the maturation of the erythroid cell.en_US
dc.format.extent412061 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleIsolation of an acid protease from rabbit reticulocytes and evidence for its role in processing redox proteins during erythroid maturationen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.identifier.pmid7028033en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/24341/1/0000608.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(81)90696-3en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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