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Science 28 July 1978:
Vol. 201. no. 4353, pp. 362 - 364
DOI: 10.1126/science.663663
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Articles

Science, Vol 201, Issue 4353, 362-364
Copyright © 1978 by American Association for the Advancement of Science

articles

Aggregation effects on oxygen binding of sickle cell hemoglobin

SJ Gill, R Skold, L Fall, T Shaeffer, P Spokane, and J Wyman

Deoxygenation of concentrated solutions (0.33 gram per milliliter) of sickle cell hemoglobin show (i) a "crisis point" where the oxygen binding curve is unusually steep (Hill coefficient of 5 to 6), and (ii) a simultaneous increase in light scattering. Nearly identical oxygen binding curves are obtained upon oxygenation and deoxygenation of these solutions. The influence of aggregation is to shift the curve toward higher pressures.


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The Structural and Functional Analysis of the Hemoglobin D Component from Chicken.
J. E. Knapp, M. A. Oliveira, Q. Xie, S. R. Ernst, A. F. Riggs, and M. L. Hackert (1999)
J. Biol. Chem. 274, 6411-6420
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