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HUMAN CARBONIC ANHYDRASES AND CARBONIC ANHYDRASE DEFICIENCIES
Annual Review of Biochemistry, 1995Carbonic anhydrases (CAs I-VII) are products of a gene family that encodes seven isozymes and several homologous, CA- related proteins. All seven isozymes have been cloned, sequenced, and mapped, and the intron-exon organization of five genes established. They differ in subcellular localizations, being cytoplasmic (CA I, II, III, and VII), GPI-anchored
W S, Sly, P Y, Hu
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ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
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AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
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American Journal of Physiology-Renal Physiology, 1982
Carbonic anhydrase is a zinc metalloenzyme widely distributed throughout the tissues of the body. This enzyme exists in a number of isozymic forms in most mammalian species. Significant advances over the past decade have been made in characterizing the nature of renal carbonic anhydrase.
D C, Dobyan, R E, Bulger
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Carbonic anhydrase is a zinc metalloenzyme widely distributed throughout the tissues of the body. This enzyme exists in a number of isozymic forms in most mammalian species. Significant advances over the past decade have been made in characterizing the nature of renal carbonic anhydrase.
D C, Dobyan, R E, Bulger
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International Journal of Biochemistry, 1987
Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms.
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Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms.
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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.
H, Fukuzawa, M, Tsuzuki, S, Miyachi
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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.
H, Fukuzawa, M, Tsuzuki, S, Miyachi
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2016
Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β-, and η-classes are present in many pathogenic protozoa, such as those belonging to the Trypanosoma, Leishmania, and Plasmodium genera. In the last years many such enzymes have been cloned, purified, and extensively characterized.
Supuran C. T., Capasso C.
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Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β-, and η-classes are present in many pathogenic protozoa, such as those belonging to the Trypanosoma, Leishmania, and Plasmodium genera. In the last years many such enzymes have been cloned, purified, and extensively characterized.
Supuran C. T., Capasso C.
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CARBONIC ANHYDRASE IN THE PREMATURE
Pediatrics, 1968Carbonic anhydrase activity was measured in the blood of premature and full-term infants to determine if the arterial-alveolar carbon dioxide gradient was related to low levels of carbonic anhydrase. The time at which levels in these infants approached the adult was studied as well.
E, Poblete, D W, Thibeault, P A, Auld
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