Inhibition of protein synthesis in cell-free systems by homocitrullylamino adenosine
dc.contributor.author | Guarino, Armand J. | en_US |
dc.contributor.author | Ibershof, Mary Lou | en_US |
dc.contributor.author | Swain, Richard R. | en_US |
dc.date.accessioned | 2006-04-13T14:52:29Z | |
dc.date.available | 2006-04-13T14:52:29Z | |
dc.date.issued | 1963 | en_US |
dc.identifier.citation | Guarino, 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.uri | http://www.sciencedirect.com/science/article/B73G7-487F7DH-3V/2/b13655764bb94d848fc1fa7d99709b9c | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32247 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13951026&dopt=citation | en_US |
dc.description.abstract | Homocitrullylamino 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.extent | 430419 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Inhibition of protein synthesis in cell-free systems by homocitrullylamino adenosine | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | The Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | The Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | The Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.identifier.pmid | 13951026 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32247/1/0000309.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0926-6550(63)90309-8 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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