Carbonic Anhydrase Activity in Intact Red Cells as Measured by Means of 18O Exchange Between CO2 and Water

1980 ◽  
pp. 177-183 ◽  
Author(s):  
R. E. Forster ◽  
N. Itada
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Red Cells

scholarly journals Enrichment of erythrocytes of fetal origin from adult-fetal blood mixtures via selective hemolysis of adult blood cells: an aid to antenatal diagnosis of hemoglobinopathies

Blood ◽  
1976 ◽  
Vol 47 (6) ◽  
pp. 883-897
Author(s):  
SH Boyer ◽  
AN Noyes ◽  
ML Boyer
Keyword(s):  
Carbonic Anhydrase ◽  
Enzyme Inhibitor ◽  
Antenatal Diagnosis ◽  
Carbonic Anhydrase Activity ◽  
Red Cells ◽  
Fetal Origin ◽  
Successful Isolation ◽  
Erythrocyte Enzyme ◽  
Erythrocyte Carbonic Anhydrase ◽  
Carbonic Anhydrase Enzyme

Red cell lysis in isotonic solutions containing NH4Cl, NH4HCO3, and a carbonic anhydrase enzyme inhibitor (acetazolamide) is a function of erythrocyte enzyme activity and permeability of cells to the inhibitor. Erythrocyte carbonic anhydrase activity is at least fivefold greater and acetazolamide permeability about tenfold less for adults than for newborns. In this setting, greater than 99.9% of red cells from adults can be hemolyzed at a time when greater than 25% of those from newborns remain intact. This easily applied method may be useful when antenatal diagnosis of hemoglobinopathies is otherwise precluded by contaimination with maternal erythrocytes. The feasibility of differential hemolysis via NH4Cl--HCO3-mediated, acetazolamide- modulated reactions is shown by the successful isolation of the few fetal-origin erythrocytes present in grossly nonbloody amniotic fluids and, in one instance, by approximately 3300-fold enrichment of apparently authentic fetal-origin red cells from the arm blood of a woman in her 18th wk of pregnancy.

scholarly journals Enrichment of erythrocytes of fetal origin from adult-fetal blood mixtures via selective hemolysis of adult blood cells: an aid to antenatal diagnosis of hemoglobinopathies

Blood ◽  
1976 ◽  
Vol 47 (6) ◽  
pp. 883-897 ◽  
Author(s):  
SH Boyer ◽  
AN Noyes ◽  
ML Boyer
Keyword(s):  
Carbonic Anhydrase ◽  
Enzyme Inhibitor ◽  
Antenatal Diagnosis ◽  
Carbonic Anhydrase Activity ◽  
Red Cells ◽  
Fetal Origin ◽  
Successful Isolation ◽  
Erythrocyte Enzyme ◽  
Erythrocyte Carbonic Anhydrase ◽  
Carbonic Anhydrase Enzyme

Abstract Red cell lysis in isotonic solutions containing NH4Cl, NH4HCO3, and a carbonic anhydrase enzyme inhibitor (acetazolamide) is a function of erythrocyte enzyme activity and permeability of cells to the inhibitor. Erythrocyte carbonic anhydrase activity is at least fivefold greater and acetazolamide permeability about tenfold less for adults than for newborns. In this setting, greater than 99.9% of red cells from adults can be hemolyzed at a time when greater than 25% of those from newborns remain intact. This easily applied method may be useful when antenatal diagnosis of hemoglobinopathies is otherwise precluded by contaimination with maternal erythrocytes. The feasibility of differential hemolysis via NH4Cl--HCO3-mediated, acetazolamide- modulated reactions is shown by the successful isolation of the few fetal-origin erythrocytes present in grossly nonbloody amniotic fluids and, in one instance, by approximately 3300-fold enrichment of apparently authentic fetal-origin red cells from the arm blood of a woman in her 18th wk of pregnancy.

scholarly journals Hypoxic incubation leads to concerted changes of carbonic anhydrase activity and 2.3 DPG concentration of chick embryo red cells

1986 ◽  
Vol 116 (2) ◽  
pp. 548-551 ◽  
Author(s):  
Rosemarie Baumann ◽  
E.A. Haller ◽  
U. Schöning ◽  
M. Weber
Keyword(s):  
Chick Embryo ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Red Cells ◽  
Hypoxic Incubation

Carbonic anhydrase activity of the cat hind leg

1979 ◽  
Vol 47 (5) ◽  
pp. 1090-1098 ◽  
Author(s):  
R. M. Effros ◽  
M. L. Weissman
Keyword(s):  
Carbonic Anhydrase ◽  
Femoral Artery ◽  
Carbonic Anhydrase Activity ◽  
Co2 Exchange ◽  
Red Cells ◽  
Venous Outflow ◽  
Perfusion Solution ◽  
Endothelial Surface ◽  
Carbonic Anhydrase Inhibition

The accessibility of tissue carbonic anhydrase to plasma was studied in five surgically isolated cat hind legs. After the leg was skinned and the paw circulation occluded with a tourniquet, it was perfused with a solution that contained neither red cells nor carbonic anhydrase. Solutions containing either H14CO3- or 14CO2 were injected with 125I-albumin, 22Na+, and 3H2O into the femoral artery and the concentrations of each were measured in the femoral venous outflow. Under control circumstances the outflow patterns of H14CO3- and 14CO2 were very similar. However, after carbonic anhydrase inhibition with 20 mg/l acetazolamide in the perfusion solution, the initial exchange of H14CO3- (“extraction”) was greatly decreased, whereas the extraction of 14CO2 was slightly increased. Because there was insignificant carbonic anhydrase activity in the venous outflow, these data suggest the presence of carbonic anhydrase at a readily accessible site, possibly bound to the endothelial surface. In this location it would promote CO2 exchange and minimize disequilibrium between plasma HCO3- and CO2.

Carbonic Anhydrase Activity During Embryonic Development

1951 ◽  
Vol 28 (3) ◽  
pp. 332-343
Author(s):  
A. M. CLARK
Keyword(s):  
Bone Marrow ◽  
Carbonic Anhydrase ◽  
Embryonic Development ◽  
Late Stage ◽  
Early Stage ◽  
Carbonic Anhydrase Activity ◽  
Red Cells ◽  
Adult Type

1. Tissue carbonic anhydrase is usually formed at an early stage in the embryonic development of the chick and mouse. The enzyme does not appear in the blood until a relatively late stage has been reached. 2. In the erythrocytes, it is probable that the enzyme is confined to those cells produced in bone marrow. 3. Evidence is presented to support the theory that towards the end of development, there is a replacement of red cells which contain an embryonic type of haemoglobin but no carbonic anhydrase, by corpuscles in which the enzyme is present together with the adult type of haemoglobin.

1123: Renal Oxalate Transport Depends on Local Carbonic Anhydrase Activity in the Proximal Tubule

2004 ◽  
Vol 171 (4S) ◽  
pp. 296-296
Author(s):  
Michael Straub ◽  
Joséphine Befolo-Elo ◽  
Richard E Hautmann ◽  
Edgar Braendle
Keyword(s):  
Carbonic Anhydrase ◽  
Proximal Tubule ◽  
Carbonic Anhydrase Activity ◽  
Oxalate Transport

scholarly journals Carbonic anhydrase activity in mitochondria from rat liver.

1982 ◽  
Vol 257 (12) ◽  
pp. 6850-6855
Author(s):  
S H Vincent ◽  
D N Silverman
Keyword(s):  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Carbonic Anhydrase Activity

Comparative study by histochemical, biochemical, and histophotometrical methods of carbonic anhydrase activity in the stomach of various vertebrate classes

1988 ◽  
Vol 84 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Pietro Palatroni ◽  
Maria Gabriella Gabrielli ◽  
Iolanda Grappasonni
Keyword(s):  
Carbonic Anhydrase ◽  
Comparative Study ◽  
Carbonic Anhydrase Activity
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