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Hadamard transform photothermal deflection desitometry of electrophretically blotted proteins

dc.contributor.authorTreado, Patrick J.en_US
dc.contributor.authorBriggs, Linda M.en_US
dc.contributor.authorMorris, Michael D.en_US
dc.date.accessioned2006-04-10T13:56:08Z
dc.date.available2006-04-10T13:56:08Z
dc.date.issued1990en_US
dc.identifier.citationTreado, Patrick J., Briggs, Linda M., Morris, Michael D. (1990)."Hadamard transform photothermal deflection desitometry of electrophretically blotted proteins." Journal of Chromatography A 511(): 341-352. <http://hdl.handle.net/2027.42/28875>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6TG8-453C16T-FV/2/7e8c16422da42e021cdaa95d6dde1545en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/28875
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2211917&dopt=citationen_US
dc.description.abstractHadamard transform spatial multiplexing techniques are applied to laser densitometry in order to prevent the photo-induced degradation of sensitive materials. Photochemical and thermal degradations can often occur in point focused scanning laser densitometry. In spatial multiplexing, the excitation source is defocused and efficiently distributed throughout the sample, reducing local power density. In this paper, we describe the application of Hadamard transform spatial multiplexing to transverse photothermal deflection spectroscopy (PDS). Proteins western blotted on nitrocellulose membrane are line imaged using the Hadamard transform PDS densitometer. For comparison, the blots are imaged with a high-dynamic-range video densitometer.en_US
dc.format.extent903342 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleHadamard transform photothermal deflection desitometry of electrophretically blotted proteinsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055 U.S.A.en_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055 U.S.A.en_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055 U.S.A.en_US
dc.identifier.pmid2211917en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/28875/1/0000710.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/S0021-9673(01)93297-2en_US
dc.identifier.sourceJournal of Chromatography Aen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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