Results 271 to 280 of about 66,240 (319)

Carbonic anhydrase II promotes cardiomyocyte hypertrophy

Canadian Journal of Physiology and Pharmacology, 2012
Pathological cardiac hypertrophy, the maladaptive remodelling of the myocardium, often progresses to heart failure. The sodium–proton exchanger (NHE1) and chloride–bicarbonate exchanger (AE3) have been implicated as important in the hypertrophic cascade.
Brittany F, Brown, Anita, Quon, Jason R B, Dyck, Joseph R, Casey   +3 more
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Expression of carbonic anhydrase IV in carbonic anhydrase II-deficient mice

American Journal of Physiology-Renal Physiology, 1997
Chronic metabolic acidosis (CMA) in the rabbit upregulates carbonic anhydrase (CA) IV in the proximal convoluted tubule (PCT). This study was designed to assess CA IV expression in a model of CMA in the mouse, i.e., congenital deficiency in CA II [CA(II)D].
L P, Brion, W, Cammer, L M, Satlin, C, Suarez, B J, Zavilowitz, V L, Schuster   +5 more
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Inhibition of carbonic anhydrase II by sulfonamide derivatives.

Die Pharmazie, 2021
A series of sulfonamide derivatives were synthesized, and the enzyme inhibitory activity of the synthesized compounds on carbonic anhydrase II was evaluated. Through molecular docking studies, it was found that compounds 1b, 1e, 2a, 2b, 3a have a strong binding affinity to carbonic anhydrase II.
Xuan, G. S., Zhan, J. H., Zhang, A. M., Li, W., Zheng, K.   +4 more
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Carbonic anhydrase activity of intact carbonic anhydrase II-deficient human erythrocytes

Journal of Applied Physiology, 1988
Intact erythrocytes from subjects with deficiency of blood carbonic anhydrase (CA) II and from normal subjects were assayed for enzyme activity by use of an 18O exchange technique in a solution containing 25 mM (CO2 + NaHCO3) plus 125 mM NaCl. At 25 degrees C and pH 7.4, the catalyzed reaction velocity was 0.32 +/- 0.04 M/s for the CA II-deficient and
S J, Dodgson, R E, Forster, W S, Sly, R E, Tashian   +3 more
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Carbonic Anhydrase II Deficiency

Clinical Orthopaedics and Related Research, 1993
Carbonic anhydrase (CA) isoenzyme II deficiency--formerly called the syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification--is an autosomal recessive "inborn error of metabolism" that has disclosed important insight concerning osteoclast function.
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Respiratory acidosis in carbonic anhydrase II-deficient mice

American Journal of Physiology-Lung Cellular and Molecular Physiology, 1998
To investigate the role of carbonic anhydrase (CA) II on pulmonary CO2exchange, we analyzed arterial blood gases from CA II-deficient and normal control mice. CA II-deficient mice had a low arterial blood pH (7.18 ± 0.06) and[Formula: see text] concentration ([[Formula: see text]]; 17.5 ± 1.9 meq/l) and a high [Formula: see text](47.4 ± 5.3 mmHg ...
Y H, Lien, L W, Lai
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Carbonic Anhydrase II Polymorphism in Africa

Human Heredity, 1972
The frequency of variant high activity human redcell carbonic anhydrase allele (CA IIh) has been examined in fourAfrican populations.The CA IIh gene frequency ranged from zero to 0.123 with amean overall value of 0.105.
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Two-Prong Inhibitors for Human Carbonic Anhydrase II

Journal of the American Chemical Society, 2004
The enzyme inhibitors are usually designed by taking into consideration the overall dimensions of the enzyme's active site pockets. This conventional approach often fails to produce desirable affinities of inhibitors for their cognate enzymes. To circumvent such constraints, we contemplated enhancing the binding affinities of inhibitors by attaching ...
Bidhan C, Roy, Abir L, Banerjee, Michael, Swanson, Xiao G, Jia, Manas K, Haldar, Sanku, Mallik, D K, Srivastava   +6 more
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A Caged Hydrophobic Inhibitor of Carbonic Anhydrase II

Organic Letters, 1999
[formula: see text] A tight-binding, hydrophobic inhibitor of carbonic anhydrase II has been masked with a water-solubilizing, photolabile group derived from o-nitrophenylglycine. This caged inhibitor represents our first effort at the site-specific delivery of prodrugs that can be activated by light.
P D, Kehayova, G E, Bokinsky, J D, Huber, A, Jain   +3 more
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Anion complexes of Cu(II) bovine carbonic anhydrase

Archives of Biochemistry and Biophysics, 1975
Abstract 1. The stability constants of some anion complexes of bovine Cu(II) carbonic anhydrase have been determined. They are found to be three-four orders of magnitude higher than those of the corresponding complexes of bovine superoxide dismutase, aqueous copper, and copper compounds of low molecular weight.
L, Morpurgo, G, Rotilio, A F, Agró, B, Mondovì   +3 more
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