## Abstract Certain anions have been shown experimentally to influence the rate of iron release from human serum transferrin (HST), implying the existence of one or more allosteric kinetically significant anionβbinding (KISAB) sites on or near the surface of the protein. A rankβordered selection of
Site selectivity in the binding of inorganic anions to serum transferrin
β Scribed by Wesley R. Harris; Diane Nesset-Tollefson; Jana Z. Stenback; Norziah Mohamed-Hani
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 618 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0162-0134
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π SIMILAR VOLUMES
Samples of monoferric human serum transferrin have been prepared in which the iron occupies predominantly the N-site (sample A) and the C-site (sample B). 111In was then added in concentrations small enough to ensure that there was always an excess of specific binding sites. Because of the presence
The resonance Raman (RR) data for a variety of transferrin samples were investigated to explore differences between the two active sites. The excitation wavelength dependence of the RR data in the low energy shift region ( Γ΅900 cm 01 ) for diferric transferrin (Fe 2 Tf) reveals extensive changes in