Show simple item record

Joining of simian virus 40 DNA molecules at endonuclease R Eco RI sites by polynucleotide ligase and analysis of the products by agarose gel electrophoresis

dc.contributor.authorDe Vries, F. A. J.en_US
dc.contributor.authorCollins, Carolyn J.en_US
dc.contributor.authorJackson, David A.en_US
dc.date.accessioned2006-04-07T16:27:27Z
dc.date.available2006-04-07T16:27:27Z
dc.date.issued1976-07-02en_US
dc.identifier.citationDe Vries, F. A. J., Collins, Carolyn J., Jackson, David A. (1976/07/02)."Joining of simian virus 40 DNA molecules at endonuclease R Eco RI sites by polynucleotide ligase and analysis of the products by agarose gel electrophoresis." Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis 435(3): 213-227. <http://hdl.handle.net/2027.42/21728>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73G8-47TG50F-131/2/b4df2e4bf4fd0f0ab416a6bef383f51cen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/21728
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=181070&dopt=citationen_US
dc.description.abstractDNA molecules cut with endonuclease R Eco RI can be joined at Eco RI cleavage sites by incubation with polynucleotide ligase. In order to define the optimum conditions for this reaction, linear Simian Virus 40 DNA molecules (SV40(LRI)) produced by endonuclease R Eco RI cleavage of SV40 form I DNA were joined using polynucleotide ligases specified by bacteriophage T4 and Escherichia coli. We have determined that the concentration of the substrate DNA molecules is the most important factor determining the distribution of covalently joined product molecules into a variety of circular and linear monomeric and oligomeric species.en_US
dc.format.extent940263 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleJoining of simian virus 40 DNA molecules at endonuclease R Eco RI sites by polynucleotide ligase and analysis of the products by agarose gel electrophoresisen_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 Microbiology, University of Michigan Medical School, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.contributor.affiliationumDepartment of Microbiology, University of Michigan Medical School, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.contributor.affiliationumDepartment of Microbiology, University of Michigan Medical School, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.identifier.pmid181070en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/21728/1/0000120.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2787(76)90103-9en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.