Results 301 to 310 of about 2,453,486 (333)
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The Role of Carbonic Anhydrase in Hepatic Glucose Production.
Current Diabetes Reviews, 2018BACKGROUND Carbonic anhydrase is a ubiquitous zinc metalloenzyme in organisms that primarily catalyzes the reversible hydration of CO2 to HCO3 - and H+.
I. Ismail
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Carbonic Anhydrase in Bacteria
Nature, 1963THE richest source of carbonic anhydrase is mammalian erythrocytes. It is also found in the pancreas, gastric mucosa, and kidney in fairly high concentration. Carbonic anhydrase has also been found localized in the cytoplasm of plant leaf tissue1–4. A survey of the literature revealed no report of the occurrence of microbial carbonic anhydrases.
F. P. Veitch, L. C. Blankenship
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Bioorganic & Medicinal Chemistry Letters, 2010
Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread enzymes in all organisms, catalyzing CO2 hydration to bicarbonate and protons. Their inhibition is exploited clinically for decades for various classes of diuretics and systemically acting antiglaucoma agents.
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Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread enzymes in all organisms, catalyzing CO2 hydration to bicarbonate and protons. Their inhibition is exploited clinically for decades for various classes of diuretics and systemically acting antiglaucoma agents.
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Carbonic Anhydrase in the Cornea
Acta Physiologica Scandinavica, 1974AbstractCarbonic anhydrase activity in the corneas of adult man, human fetus, monkey, rabbit, rat, cow, pig and American bullfrog was examined by the histochemical method of Hansson. In all species the endothelial cells were intensely and distinctly stained for carbonic anhydrase activity.
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2000
Microalgae grown in ordinary air (0.04% CO2) show a much higher affinity for inorganic carbon (Ci) in photosynthesis than those grown with 2% to 5% CO2, although at saturating CO2 concentrations the maximum rate of photosynthesis is almost the same.
Hideya Fukuzawa +2 more
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Microalgae grown in ordinary air (0.04% CO2) show a much higher affinity for inorganic carbon (Ci) in photosynthesis than those grown with 2% to 5% CO2, although at saturating CO2 concentrations the maximum rate of photosynthesis is almost the same.
Hideya Fukuzawa +2 more
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Nature, 1947
IN contrast to the wealth of information concerning carbonic anhydrase in the animal kingdom, there have been few reports of the occurrence of this enzyme in the plant kingdom1. It seemed desirable, therefore, briefly to describe the following observations made in the course of work on the enzyme in animal tissues.
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IN contrast to the wealth of information concerning carbonic anhydrase in the animal kingdom, there have been few reports of the occurrence of this enzyme in the plant kingdom1. It seemed desirable, therefore, briefly to describe the following observations made in the course of work on the enzyme in animal tissues.
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1987
The ṗroperties of Carbonic Anhydrase, the enzyme which catalyzes the CO2 hydration and HCO3 - dehydration, are reviewed. The mechanism is discussed in details in terms of Zn-OH attacking CO2 to give rise to HCO3 which is then released after H20 uptake. H+ is then released. The inhibition mechanism is also discussed.
BERTINI, IVANO +2 more
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The ṗroperties of Carbonic Anhydrase, the enzyme which catalyzes the CO2 hydration and HCO3 - dehydration, are reviewed. The mechanism is discussed in details in terms of Zn-OH attacking CO2 to give rise to HCO3 which is then released after H20 uptake. H+ is then released. The inhibition mechanism is also discussed.
BERTINI, IVANO +2 more
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Accelerating Mineral Carbonation Using Carbonic Anhydrase.
Environmental Science and Technology, 2016Carbonic anhydrase (CA) enzymes have gained considerable attention for their potential use in carbon dioxide (CO2) capture technologies because they are able to catalyze rapidly the interconversion of aqueous CO2 and bicarbonate.
I. Power, A. Harrison, G. Dipple
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Novel Carbonic Anhydrase Inhibitors
Future Medicinal Chemistry, 2021Abstract
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1991
Carbonic anhydrase (CA) (EC 4.2.1.1.) was first characterized in erythrocytes in 1933 directly as a result of a search by several laboratories for a catalytic factor in the erythrocytes that had been theoretically determined as necessary for rapid transit of the HCO 3 − from the erythrocyte to the pulmonary capillary.
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Carbonic anhydrase (CA) (EC 4.2.1.1.) was first characterized in erythrocytes in 1933 directly as a result of a search by several laboratories for a catalytic factor in the erythrocytes that had been theoretically determined as necessary for rapid transit of the HCO 3 − from the erythrocyte to the pulmonary capillary.
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