Inhibition by anions of human red cell carbonic anhydrase B: physiological and biochemical implications

Science ◽  
2003 ◽  
Vol 191 (4226) ◽  
pp. 469-472 ◽  
Author(s):  
T. Maren ◽  
C. Rayburn ◽  
N. Liddell
Keyword(s):  
Carbonic Anhydrase ◽  
Red Cell ◽  
Carbonic Anhydrase B ◽  
Physiological And Biochemical

scholarly journals Enzymatically Inactive Red Cell Carbonic Anhydrase B in a Family with Renal Tubular Acidosis

1974 ◽  
Vol 53 (1) ◽  
pp. 59-63 ◽  
Author(s):  
Emmanuel Shapira ◽  
Yoav Ben-Yoseph ◽  
Fabien G. Eyal ◽  
Alexander Russell
Keyword(s):  
Carbonic Anhydrase ◽  
Renal Tubular Acidosis ◽  
Red Cell ◽  
Carbonic Anhydrase B ◽  
Renal Tubular

RED CELL ZINC AND RED CELL ZINC METALLOENZYMES IN HYPERTHYROIDISM

1974 ◽  
Vol 76 (3) ◽  
pp. 645-650 ◽  
Author(s):  
J. A. Pangaro ◽  
M. Weinstein ◽  
M. C. Devetak ◽  
R. J. Soto
Keyword(s):  
Carbonic Anhydrase ◽  
Alcohol Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Control Group ◽  
Red Cell ◽  
Malic Dehydrogenase ◽  
Carbonic Anhydrase B ◽  
Zinc Metalloenzymes ◽  
The Mean ◽  
Hyperthyroid Patients

ABSTRACT The activity of the following zinc metalloenzymes was measured in the erythrocytes of hyperthyroid patients: malic dehydrogenase (MDH), aldolase (ALD), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), alcohol dehydrogenase (ADH), and lactic dehydrogenase (LDH). A significant increase in the activities of ADH (0.8 ± 0.3 μmoles per min per g of haemoglobin) and GAPDH (30.5 ± 13.4) was found; the control values being 0.5 ± 0.3 and 7.6 ± 4.6 respectively. The activities of ALD, MDH, and of LDH were not significantly different from those of the control group. The mean red cell zinc in the hyperthyroid group was 31.6 ± 6.2 μg per g of haemoglobin in contrast to 50.4 ± 8.1 in the control group. It is concluded that none of the zinc metalloenzymes measured accounts for the diminution of erythrocyte zinc occurring in hyperthyroidism, a phenomenon that should be attributed to the inhibition of carbonic anhydrase B as reported previously.

Time course of exchanges between red cells and extracellular fluid during CO2 uptake

1975 ◽  
Vol 38 (4) ◽  
pp. 710-718 ◽  
Author(s):  
R. E. Forster ◽  
E. D. Crandall
Keyword(s):  
Carbonic Anhydrase ◽  
Time Course ◽  
Extracellular Fluid ◽  
Extracellular Ph ◽  
Co2 Uptake ◽  
Sudden Increase ◽  
Red Cell ◽  
Ph Change ◽  
Red Cell Membrane

A stopped-flow rapid-reaction apparatus was used to follow the time course of extracellular pH in a human red cell suspension following a sudden increase in PCO2. The extracellular pH change was slow (t1/2 similar to 3.5 s) considering the presence of carbonic anhydrase in the cells. When carbonic anhydrase was added to the extracellular fluid, the half-time was reduced to less than 20 ms. The explanation for these phenomena is that the equilibration of H+ across the red cell membrane is rate-limited by the uncatalyzed reaction CO2 plus H2O formed from H2CO3 outside the cells. A theoretical model was developed which successfully reproduced the experimental results. When the model was used to simulate CO2 exchange in vivo, it was determined that blood PCO2 and pH require long times (greater than 50 s) to approach equilibrium between cells and plasma after leaving an exchange capillary. We conclude that cell-plasma equilibrium may never be reached in vivo, and that in vitro measurements of these quantities may not represent their true values at the site of sampling.

Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization

1990 ◽  
Vol 213 (3) ◽  
pp. 561-568 ◽  
Author(s):  
G.V. Semisotnov ◽  
V.N. Uversky ◽  
I.V. Sokolovsky ◽  
A.M. Gutin ◽  
O.I. Razgulyaev ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase ◽  
Proline Isomerization ◽  
Carbonic Anhydrase B
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