The electrophoresis of transferrins in urea/polyacrylamide gels

Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/4340

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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

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