Please use this identifier to cite or link to this item: http://buratest.brunel.ac.uk/handle/2438/4340
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dc.contributor.authorEvans, RW-
dc.contributor.authorWilliams, J-
dc.date.accessioned2010-05-13T11:49:18Z-
dc.date.available2010-05-13T11:49:18Z-
dc.date.issued1980-
dc.identifier.citationBiochemical Journal. 189: 541-546en
dc.identifier.issn0264-6021-
dc.identifier.urihttp://bura.brunel.ac.uk/handle/2438/4340-
dc.description.abstractThe denaturation of transferrin by urea has been studied by (a) electrophoresis in polyacrylamide gels incorporating a urea gradient, (b) measurements of the loss in iron-binding capacity and (c) u.v. difference spectrometry. In human serum transferrin and hen ovotransferrin the N-terminal and C-terminal domains of the iron-free protein were found to denature at different urea concentrations.en
dc.language.isoenen
dc.publisherPortland Pressen
dc.titleThe electrophoresis of transferrins in urea/polyacrylamide gelsen
dc.typeArticleen
Appears in Collections:Biological Sciences
Dept of Life Sciences Research Papers

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