Analysis of the Iron-Binding Sites of Transferrin by Isoelectric Focussing
- 1 January 1978
- journal article
- research article
- Published by Walter de Gruyter GmbH in cclm
- Vol. 16 (10), 557-60
- https://doi.org/10.1515/cclm.1978.16.10.557
Abstract
1. Human transferrin was labelled with ferric nitrilotriacetate (FeNTA) at one of its two metal binding sites by variation of the pH. 2. Four transferrin forms, transferrin, transferrin(Fe) (A-site), transferrin(Fe) (B-site) and transferrin(2Fe) could be separated on flat bed gels by isoelectric focussing. 3. Incubation time, temperature and medium play an important role in the specificity of the binding of Fe. In NTA-pH-buffer, at 0.5 Fe-saturation, the A-site was preferentially labelled at pH 7--8, the B-site at a pH 8--9. 4. Under physiological conditions iron from the B-site has the tendency to move to the A-site.Keywords
This publication has 11 references indexed in Scilit:
- A new staining technique for proteins in polyacrylamide gels using Coomassie brilliant blue G250Analytical Biochemistry, 1977
- Functional equivalence of iron bound to human transferrin at low pH or high pHBiochimica et Biophysica Acta (BBA) - General Subjects, 1977
- Functional heterogeneity and pH-dependent dissociation properties of human transferrinBiochimica et Biophysica Acta (BBA) - General Subjects, 1976
- The Effect of pH upon Human Transferrin: Selective Labelling of the Two Iron‐binding SitesBritish Journal of Haematology, 1976
- Nonequivalence of the metal binding sites in vanadyl-labeled human serum transferrinBiochemistry, 1975
- Functional equivalence of the two iron-binding sites of human transferrinNature, 1975
- Difference between the two iron-binding sites of transferrinNature, 1975
- Iron-donating properties of transferrinBiochemistry, 1975
- Function of TransferrinNature, 1968
- Significance of the Binding of Iron by TransferrinNature, 1967