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Inhibition of protein synthesis in cell-free systems by homocitrullylamino adenosine

dc.contributor.authorGuarino, Armand J.en_US
dc.contributor.authorIbershof, Mary Louen_US
dc.contributor.authorSwain, Richard R.en_US
dc.date.accessioned2006-04-13T14:52:29Z
dc.date.available2006-04-13T14:52:29Z
dc.date.issued1963en_US
dc.identifier.citationGuarino, Armand J., Ibershof, Mary Lou, Swain, Richard (1963)."Inhibition of protein synthesis in cell-free systems by homocitrullylamino adenosine." Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects 72(): 62-68. <http://hdl.handle.net/2027.42/32247>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73G7-487F7DH-3V/2/b13655764bb94d848fc1fa7d99709b9cen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32247
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13951026&dopt=citationen_US
dc.description.abstractHomocitrullylamino adenosine inhibits the incorporation of [14C]amino acids into a hot acid-insoluble form in cell-free systems derived from Escherichia coli and rat liver. The concentration necessary for one-half maximal inhibition in the E. coli system is 1.1[middle dot]10-4 M. Addition of the intact molecule is necessary for the maximum inhibition. The inhibition does not appear to involve the activation of the amino acids or their transfer to s-RNA, but rather exerts its effect, like puromycin, at the level involving the s-RNA ribosomal complex.en_US
dc.format.extent430419 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleInhibition of protein synthesis in cell-free systems by homocitrullylamino adenosineen_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.affiliationumThe Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.contributor.affiliationumThe Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.contributor.affiliationumThe Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.identifier.pmid13951026en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32247/1/0000309.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0926-6550(63)90309-8en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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