Evidence for Multiple Differing Cation Binding Sites on Hemoglobin A and S
- 1 January 1981
- journal article
- research article
- Published by Taylor & Francis in Hemoglobin
- Vol. 5 (3), 231-240
- https://doi.org/10.3109/03630268108997547
Abstract
Some divalent cations (at 10-3 M concentration) act as oxygen-linked ligands. The effect of Ca2+ (on Hb S) and Zn2+ (on Hb A and Hb S) can be traced to a preferential binding of these cations to the oxy- conformation of the proteins; the reverse is true for Ni2+, since its presence reduces the oxygen affinity of both Hb. Hb apparently has at least 2 different cation binding sites. The replacement of glutamic acid by valine in Hb S apparently introduces sufficient structural modification to form a new cation binding site.This publication has 22 references indexed in Scilit:
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