Temperature Transition of Human Hemoglobin at Body Temperature: Effects of Calcium
We studied the effects of calcium ion concentration on the temperature dependence of rheological behavior of human red blood cells (RBCs) and concentrated hemoglobin solutions. Our previous study (G. M. Artmann, C. Kelemen, D. Porst, G. Büldt, and S. Chien, 1998, Biophys. J., 75:3179–3183) showed a...
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Published in | Biophysical journal Vol. 80; no. 6; pp. 2622 - 2630 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.06.2001
Biophysical Society |
Subjects | |
Online Access | Get full text |
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Summary: | We studied the effects of calcium ion concentration on the temperature dependence of rheological behavior of human red blood cells (RBCs) and concentrated hemoglobin solutions. Our previous study (G. M. Artmann, C. Kelemen, D. Porst, G. Büldt, and S. Chien, 1998,
Biophys. J., 75:3179–3183) showed a critical temperature (
T
c) of 36.4
±
0.3°C at which the RBCs underwent a transition from non-passage to passage through 1.3-
μm micropipettes in response to an aspiration pressure of −2.3
kPa. An increase in intracellular Ca
2+ concentration by using the ionophore A23187 reduced the passability of intact RBCs through small micropipettes above
T
c; the micropipette diameter needed for >90% passage increased to 1.7
μm. Viscometry of concentrated hemoglobin solutions (45 and 50
g/dl) showed a sudden viscosity transition at 36
±
1°C (
T
c
η
) at all calcium concentrations investigated. Below
T
c
η
, the viscosity value of the concentrated hemoglobin solution at 1.8
mM Ca
2+ was higher than that at other concentrations (0.2
μM, 9
mM, and 18
mM). Above
T
c
η
, the viscosity was almost Ca
2+ independent. At 1.8
mM Ca
2+ and 36
±
1°C, the activation energy calculated from the viscometry data showed a strong dependence on the hemoglobin concentration. We propose that the transition of rheological behavior is attributable to a high-to-low viscosity transition mediated by a partial release of the hemoglobin-bound water. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0006-3495 1542-0086 |
DOI: | 10.1016/S0006-3495(01)76232-7 |