The electrophoresis of transferrins in urea/polyacrylamide gels
Copyright policy )The electrophoresis of transferrins in urea/polyacrylamide gels
The denaturation of transferrin by urea has been studied by (a) electrophoresis in polyacrylamide gels incorporating a urea gradient, (b) measurements of the loss of 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.
- University of Bristol United Kingdom
- Brunel University London United Kingdom
Protein Denaturation, Iron, Transferrin, 610, 630, Animals, Humans, Urea, Electrophoresis, Polyacrylamide Gel, Spectrophotometry, Ultraviolet, Chickens, Conalbumin, Protein Binding
Protein Denaturation, Iron, Transferrin, 610, 630, Animals, Humans, Urea, Electrophoresis, Polyacrylamide Gel, Spectrophotometry, Ultraviolet, Chickens, Conalbumin, Protein Binding
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