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Direct expression of active spinach glycolate oxidase in Escherichia coli
dc.contributor.authorMacheroux, Peteren_US
dc.contributor.authorMulrooney, Scott B.en_US
dc.contributor.authorWilliams, Charles H., Jr.en_US
dc.contributor.authorMassey, Vincenten_US
dc.date.accessioned2006-04-10T15:07:09Z
dc.date.available2006-04-10T15:07:09Z
dc.date.issued1992-08-17en_US
dc.identifier.citationMacheroux, Peter, Mulrooney, Scott B., Williams, Jr., Charles H., Massey, Vincent (1992/08/17)."Direct expression of active spinach glycolate oxidase in Escherichia coli." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1132(1): 11-16. <http://hdl.handle.net/2027.42/29898>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1V-47S6B5B-S3/2/4ee978324ebca964897ca02374d32f91en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/29898
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1324737&dopt=citationen_US
dc.description.abstractSpinach glycolate oxidase (GAO) was expressed in Escherichia coli using the T7 RNA polymerase promotor. The enzyme accounts for approx. 1% of the soluble protein fraction and is expressed as a soluble and active enzyme. Comparison with GAO expressed in Saccharomyces cerevisiae (Macheroux, P., Massey, V., Thiele, D.J. and Volokita, M. (1991) Biochemistry 30, 4612-4619) showed that the GAO expressed in E. coli has identical physico-chemical features to the wild-type enzyme, but is expressed at a level approx. 15-fold higher than in the yeast system.en_US
dc.format.extent597951 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleDirect expression of active spinach glycolate oxidase in Escherichia colien_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherDepartment of Veterans Affairs Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherDepartment of Veterans Affairs Medical Center, Ann Arbor, MI, USAen_US
dc.identifier.pmid1324737en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/29898/1/0000255.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0167-4781(92)90046-3en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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