Analysis of the iron-binding sites of transferrin by isoelectric focussing

van Eijk, H.G.; van Noort, W.L.; Kroos, M.J.; van der Heul, C.

Journal of Clinical Chemistry and Clinical Biochemistry 16(10): 557-560

1978


ISSN/ISBN: 0340-076X
PMID: 30806
Document Number: 131130
Human transferrin was labeld with ferric nitrilotriacetate (FeNTA) at 1 of its 2 metal binding sites by variation of the pH. Four transferrin forms, transferrin, transferrin(Fe) (A-site), transferrin(Fe) (B-site) and transferrin(2Fe) were separated on flat bed gels by isoelectric focusing. 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 labeled at pH 7-8, the B-site at a pH 8-9. Under physiological conditions Fe from the B-site has the tendency to move to the A-site.

Document emailed within 1 workday
Secure & encrypted payments