Results 241 to 250 of about 75,270 (295)
Some of the next articles are maybe not open access.
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
openaire +3 more sources
ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
openaire +3 more sources
AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
openaire +3 more sources
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.
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Future Medicinal Chemistry, 2018
Mammalian carbonic anhydrases (CAs; EC 4.2.1.1) of which 16 isoforms are known, are involved in important physiological functions. Their inhibition is exploited pharmacologically for the treatment of many diseases (glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, etc.) but the activators were less investigated till recently.
openaire +3 more sources
Mammalian carbonic anhydrases (CAs; EC 4.2.1.1) of which 16 isoforms are known, are involved in important physiological functions. Their inhibition is exploited pharmacologically for the treatment of many diseases (glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, etc.) but the activators were less investigated till recently.
openaire +3 more sources
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.
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +2 more sources
Carbonic Anhydrases An Overview
Current Pharmaceutical Design, 2008Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread metalloenzymes all over the phylogenetic tree, with at least 4 distinct gene families encoding for them. At least 16 different alpha-CA isoforms were isolated in mammals, where these enzymes play crucial physiological roles.
openaire +3 more sources
2016
Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade enzymes from Neisseria spp., Helicobacter pylori, Escherichia coli, Mycobacterium tuberculosis, Brucella spp ...
Capasso C., Supuran C. T.
openaire +1 more source
Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade enzymes from Neisseria spp., Helicobacter pylori, Escherichia coli, Mycobacterium tuberculosis, Brucella spp ...
Capasso C., Supuran C. T.
openaire +1 more source