Publication Cover
Hemoglobin
international journal for hemoglobin research
Volume 5, 1981 - Issue 3
7
Views
2
CrossRef citations to date
0
Altmetric
Original Article

Evidence for Multiple Differing Cation Binding Sites on Hemoglobin A and S

, , , , &
Pages 231-240 | Received 08 Apr 1980, Accepted 12 Sep 1980, Published online: 07 Jul 2009
 

Abstract

Some divalent cations (at 10−3M concentration) have been shown to act as oxygen-linked ligands. The effect of Ca++ (only on hemoglobin S) and Zn++ (on normal hemoglobin and hemoglobin S) can be traced to a preferential binding of these cations to the oxy- conformation of the proteins; the reverse is true for Ni++, since its presence reduces the oxygen affinity of both hemoglobins. The results suggest: i) the existence of at least two different cation binding sites on hemoglobin; ii) the replacement of glutamic acid by valine in hemoglobins S introduces sufficient structural modification to form a new cation binding site.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.