Results 251 to 260 of about 75,270 (295)
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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 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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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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Novel Carbonic Anhydrase Inhibitors
Future Medicinal Chemistry, 2021Abstract
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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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2019
Among the seven different classes of carbonic anhydrases (CAs), the Ζ-class represents a very interesting one due to the biochemical peculiarity of CDCA1, which is the most investigated representative. In fact, CDCA1 is a cambialistic enzyme being able to naturally exchange Zn(II) with Cd(II) and vice versa, within its catalytic site.
Langella, E. +4 more
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Among the seven different classes of carbonic anhydrases (CAs), the Ζ-class represents a very interesting one due to the biochemical peculiarity of CDCA1, which is the most investigated representative. In fact, CDCA1 is a cambialistic enzyme being able to naturally exchange Zn(II) with Cd(II) and vice versa, within its catalytic site.
Langella, E. +4 more
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Perspectives on carbonic anhydrase
Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 2010In the years since Larimer and Schmidt-Nielsen published their examination of red blood cell (RBC) carbonic anhydrase (CA) activities as a function of body mass in mammals, our knowledge of CA has expanded dramatically. We are now aware of the diversity of CA isoforms and their implication in a wide array of physiological processes.
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Introduction to the carbonic anhydrases
2000Since the discovery, almost 70 years ago, of the enzyme carbonic anhydrase (CA), which plays an important role in the red blood cell by catalyzing the hydration of carbon dioxide (CO2 + H2O ↔ HCO– 3+ H+), a fascinating and complex story has unfolded of three enzyme families performing numerous functions in many different organisms.
W R, Chegwidden, N D, Carter
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2000
In contrast to animal and plant carbonic anhydrases, relatively little is known about carbonic anhydrases in bacteria. Carbonic anhydrase activity has been well documented in a few bacterial species and its presence has been inferred on the basis of gene sequence homologies in several others, but their functions are generally not known.
E I, Kozliak +3 more
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In contrast to animal and plant carbonic anhydrases, relatively little is known about carbonic anhydrases in bacteria. Carbonic anhydrase activity has been well documented in a few bacterial species and its presence has been inferred on the basis of gene sequence homologies in several others, but their functions are generally not known.
E I, Kozliak +3 more
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Carbonic Anhydrase II Deficiency
Clinical Orthopaedics and Related Research, 1993Carbonic 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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