Please use this identifier to cite or link to this item:
http://bura.brunel.ac.uk/handle/2438/4340
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Evans, RW | - |
dc.contributor.author | Williams, J | - |
dc.date.accessioned | 2010-05-13T11:49:18Z | - |
dc.date.available | 2010-05-13T11:49:18Z | - |
dc.date.issued | 1980 | - |
dc.identifier.citation | Biochemical Journal. 189: 541-546 | en |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/4340 | - |
dc.description.abstract | The 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.iso | en | en |
dc.publisher | Portland Press | en |
dc.title | The electrophoresis of transferrins in urea/polyacrylamide gels | en |
dc.type | Article | en |
Appears in Collections: | Biological Sciences Dept of Life Sciences Research Papers |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
biochemj-1980.pdf | 1.39 MB | Adobe PDF | View/Open |
Items in BURA are protected by copyright, with all rights reserved, unless otherwise indicated.