A cytosolic carbonic anhydrase isoenzyme found widely distributed in cells of almost all tissues. Deficiencies of carbonic anhydrase II produce a syndrome characterized by OSTEOPETROSIS, renal tubular acidosis (ACIDOSIS, RENAL TUBULAR) and cerebral calcification. EC 4.2.1.-
A family of zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide. They play an important role in the transport of CARBON DIOXIDE from the tissues to the LUNG. EC
A class of compounds that reduces the secretion of H+ ions by the proximal kidney tubule through inhibition of CARBONIC ANHYDRASES.
A cytosolic carbonic anhydrase isoenzyme primarily expressed in skeletal muscle (MUSCLES, SKELETAL). EC 4.2.1.-
A carbonic anhydrase inhibitor used as diuretic and in glaucoma. It may cause hypokalemia.
One of the CARBONIC ANHYDRASE INHIBITORS that is sometimes effective against absence seizures. It is sometimes useful also as an adjunct in the treatment of tonic-clonic, myoclonic, and atonic seizures, particularly in women whose seizures occur or are exacerbated at specific times in the menstrual cycle. However, its usefulness is transient often because of rapid development of tolerance. Its antiepileptic effect may be due to its inhibitory effect on brain carbonic anhydrase, which leads to an increased transneuronal chloride gradient, increased chloride current, and increased inhibition. (From Smith and Reynard, Textbook of Pharmacology, 1991, p337)
A cytosolic carbonic anhydrase isoenzyme primarily expressed in ERYTHROCYTES, vascular endothelial cells, and the gastrointestinal mucosa. EC 4.2.1.-
A membrane-bound carbonic anhydrase found in lung capillaries and kidney.
A carbonic anhydrase inhibitor that is used as a diuretic and in the treatment of glaucoma.
A group of genetic disorders of the KIDNEY TUBULES characterized by the accumulation of metabolically produced acids with elevated plasma chloride, hyperchloremic metabolic ACIDOSIS. Defective renal acidification of URINE (proximal tubules) or low renal acid excretion (distal tubules) can lead to complications such as HYPOKALEMIA, hypercalcinuria with NEPHROLITHIASIS and NEPHROCALCINOSIS, and RICKETS.
Excessive formation of dense trabecular bone leading to pathological fractures; OSTEITIS; SPLENOMEGALY with infarct; ANEMIA; and extramedullary hemopoiesis (HEMATOPOIESIS, EXTRAMEDULLARY).
Inorganic salts that contain the -HCO3 radical. They are an important factor in determining the pH of the blood and the concentration of bicarbonate ions is regulated by the kidney. Levels in the blood are an index of the alkali reserve or buffering capacity.
Selective renal carbonic anhydrase inhibitor. It may also be of use in certain cases of respiratory failure.
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
Carbonic acid (H2C03). The hypothetical acid of carbon dioxide and water. It exists only in the form of its salts (carbonates), acid salts (hydrogen carbonates), amines (carbamic acid), and acid chlorides (carbonyl chloride). (From Grant & Hackh's Chemical Dictionary, 5th ed)
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group.
Proteins that cotransport sodium ions and bicarbonate ions across cellular membranes.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
An essential amino acid that is required for the production of HISTAMINE.
Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion.
The rate dynamics in chemical or physical systems.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Acute or chronic INFLAMMATION of the PANCREAS due to excessive ALCOHOL DRINKING. Alcoholic pancreatitis usually presents as an acute episode but it is a chronic progressive disease in alcoholics.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A carbonic anhydrase isoenzyme found in MITOCHONDRIA where it provides bicarbonate ions that are components in the urea cycle and in GLUCONEOGENESIS.
A group of compounds that contain the structure SO2NH2.
Esterases are hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into alcohols and acids, playing crucial roles in various biological processes including metabolism and detoxification.
Acrolein is an unsaturated aldehyde (C3H4O), highly reactive, toxic and naturally occurring compound that can be found in certain foods, tobacco smoke and is produced as a result of environmental pollution or industrial processes.
Transforming proteins encoded by erbA oncogenes from the avian erythroblastosis virus. They are truncated versions of c-erbA, the thyroid hormone receptor (RECEPTORS, THYROID HORMONE) that have retained both the DNA-binding and hormone-binding domains. Mutations in the hormone-binding domains abolish the transcriptional activation function. v-erbA acts as a dominant repressor of c-erbA, inducing transformation by disinhibiting proliferation.
A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Membrane transporters that co-transport two or more dissimilar molecules in the opposite direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Calcium, carbonic anhydrase and gastric acid secretion. (1/207)

Previous data concerning the action of calcium (Ca) on gastric acid secretion (GAS) indicated that calcium ions increase GAS elicited by gastrin released through a vagal mechanism, and also by a direct effect on parietal cells. Our research showed that the stimulating effect of calcium on gastric acid secretion can be antagonized by verapamil administration, which reduces gastric acid secretion . In the present study we followed the effect induced by administration of calcium and Ca-chelating agents (disodium EDTA) on gastric acid secretion and on carbonic anhydrase (CA) activity. We selected two groups of healthy volunteers: Group I (n=21) received a single i.v. dose of CaCl2 (15 mg/kg b.w.), whereas Group II (n=22) received a single i.v. dose of disodium EDTA (5 mg/kg b.w.). We determined blood calcium before and after treatment, gastric acid secretion at 2 hours. erythrocyte CA II activity, and CA IV activity in membrane parietal cells, which were isolated from gastric mucosa obtained by endoscopic biopsy. Assessment of carbonic anhydrase activity was achieved by the stopped-flow method. In Group I calcium administration increased blood calcium, HCl output, CA II and CA IV activity as compared to initial values. In Group II, disodium EDTA reduced blood calcium, HCl output, CA II and CA IV activity as compared to initial values. The results demonstrated that increased blood calcium and GAS values after calcium administration correlated with the increase of erythrocyte CA II and parietal cell CA IV activity, while disodium EDTA induced a reversed process. Our results also show that cytosolic CA II and membrane CA IV values are sensitive to calcium changes and they directly depend on these levels. Our data suggest that intra- and extracellular pH changes induced by carbonic anhydrase might account for the modulation of the physiological and pathological secretory processes in the organism.  (+info)

A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers. (2/207)

The cytoplasmic carboxyl-terminal domain of AE1, the plasma membrane chloride/bicarbonate exchanger of erythrocytes, contains a binding site for carbonic anhydrase II (CAII). To examine the physiological role of the AE1/CAII interaction, anion exchange activity of transfected HEK293 cells was monitored by following the changes in intracellular pH associated with AE1-mediated bicarbonate transport. AE1-mediated chloride/bicarbonate exchange was reduced 50-60% by inhibition of endogenous carbonic anhydrase with acetazolamide, which indicates that CAII activity is required for full anion transport activity. AE1 mutants, unable to bind CAII, had significantly lower transport activity than wild-type AE1 (10% of wild-type activity), suggesting that a direct interaction was required. To determine the effect of displacement of endogenous wild-type CAII from its binding site on AE1, AE1-transfected HEK293 cells were co-transfected with cDNA for a functionally inactive CAII mutant, V143Y. AE1 activity was maximally inhibited 61 +/- 4% in the presence of V143Y CAII. A similar effect of V143Y CAII was found for AE2 and AE3cardiac anion exchanger isoforms. We conclude that the binding of CAII to the AE1 carboxyl-terminus potentiates anion transport activity and allows for maximal transport. The interaction of CAII with AE1 forms a transport metabolon, a membrane protein complex involved in regulation of bicarbonate metabolism and transport.  (+info)

Estrogen regulation of ion transporter messenger RNA levels in mouse efferent ductules are mediated differentially through estrogen receptor (ER) alpha and ER beta. (3/207)

Earlier studies have shown that the efferent ductules (ED) of the male mouse are a target for estrogen. The loss of estrogen receptor (ER) function through either knockout technology (alpha ERKO mouse) or chemical interference (pure antagonist, ICI 182 780) results in a failure of a major function of the ED, the reabsorption of testicular fluids. The purpose of this study was to test the hypothesis that estrogen controls fluid (water) reabsorption in the ED by modulating ion transporters important for passive water movement through a leaky epithelium such as the ED. Northern blot analysis was used to detect the mRNA levels for key ion transporters in the following experimental groups: 1) wild-type (WT) control for the 14-day experiment, 2) ER alpha knockout (alpha ERKO) control for the 14-day experiment, 3) WT treated with ICI 182 780 (ICI) for 14 days, 4) alpha ERKO treated with ICI for 14 days, 5) WT control for the 35-day experiment, and 6) WT treated with ICI for 35 days. Estrogen differentially modulated the mRNA levels of key ion transporters. ER alpha mediated carbonic anhydrase II mRNA abundance, and there was a decrease in Na(+)/H(+) exchanger 3 mRNA levels in the alpha ERKO that appeared to be a cellular effect and not a direct estrogen effect. The loss of ER alpha control resulted in an increase in mRNA abundance for the catalytic subunit of Na(+)-K(+) ATPase alpha 1, whereas an increase in the mRNA abundance of the Cl(-)/HCO(3)(-) exchanger and the chloride channel cystic fibrosis transmembrane regulator was significantly ER beta mediated. Our results indicate for the first time that estrogen acting directly and indirectly through both ER alpha and ER beta probably modulates fluid reabsorption in the adult mouse ED by regulating the expression of ion transporters involved in the movement of Na(+) and Cl(-).  (+info)

Estrogen action and male fertility: roles of the sodium/hydrogen exchanger-3 and fluid reabsorption in reproductive tract function. (4/207)

Estrogen receptor alpha (ER alpha) is essential for male fertility. Its activity is responsible for maintaining epithelial cytoarchitecture in efferent ductules and the reabsorption of fluid for concentrating sperm in the head of the epididymis. These discoveries and others have helped to establish estrogen's bisexual role in reproductive importance. Reported here is the molecular mechanism to explain estrogen's role in fluid reabsorption in the male reproductive tract. It is shown that estrogen regulates expression of the Na(+)/H(+) exchanger-3 (NHE3) and the rate of (22)Na(+) transport, sensitive to an NHE3 inhibitor. Immunohistochemical staining for NHE3, carbonic anhydrase II (CAII), and aquaporin-I (AQP1) was decreased in ER alpha knockout (alpha ERKO) efferent ductules. Targeted gene-deficient mice were compared with alpha ERKO, and the NHE3 knockout and CAII-deficient mice showed alpha ERKO-like fluid accumulation, but only the NHE3 knockout and alpha ERKO mice were infertile. Northern blot analysis showed decreases in mRNA for NHE3 in alpha ERKO and antiestrogen-treated mice. The changes in AQP1 and CAII in alpha ERKO seemed to be secondary because of the disruption of apical cytoarchitecture. Ductal epithelial ultrastructure was abnormal only in alpha ERKO mice. Thus, in the male, estrogen regulates one of the most important epithelial ion transporters and maintains epithelial morphological differentiation in efferent ductules of the male, independent of its regulation of Na(+) transport. Finally, these data raise the possibility of targeting ER alpha in developing a contraceptive for the male.  (+info)

Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate. (5/207)

The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the widely used anti-epileptic drug topiramate, possesses anti-convulsant and carbonic anhydrase-inhibitory activities. We have studied the binding interactions of RWJ-37497 in the active site of human carbonic anhydrase II by X-ray crystallography. The atomic positions of the enzyme inhibitor complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final crystallographic R and R(free) values of 0.18 and 0.23, respectively. The inhibitor co-ordinates to the active-site zinc ion through its oxygen atom and the ionized nitrogen atom of the sulphamate group by replacing the metal-bound water molecules, although the sulphamoyl oxygen atom provides a rather lengthy co-ordination. The 4,5-cyclic sulphate group is positioned in a hydrophobic pocket of the active site, making contacts with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand was found to be intact, concerns about RWJ-37947 irreversibly alkylating the enzyme through its 4,5-cyclic sulphate group were dispelled.  (+info)

Combinatorial computational method gives new picomolar ligands for a known enzyme. (6/207)

Combinatorial small molecule growth algorithm was used to design inhibitors for human carbonic anhydrase II. Two enantiomeric candidate molecules were predicted to bind with high potency (with R isomer binding stronger than S), but in two distinct conformations. The experiments verified that computational predictions concerning the binding affinities and the binding modes were correct for both isomers. The designed R isomer is the best-known inhibitor (K(d) approximately 30 pM) of human carbonic anhydrase II.  (+info)

In vivo repression of an erythroid-specific gene by distinct corepressor complexes. (7/207)

To assess the mechanisms of repression of the erythroid-specific carbonic anhydrase II (CAII) locus we used chromatin immunoprecipitation and show that an NCoR-histone deacetylase (HDAC)3 complex is recruited by the nuclear receptor v-ErbA to the intronic HS2 enhancer turning it into a potent silencer. Furthermore we demonstrate that efficient CAII silencing requires binding of a MeCP2-targeted HDAC-containing corepressor complex to the hypermethylated CpG-island at the promoter. Activation of transcription by either AZAdC or thyroid hormone results in loss of one of the two corepressor complexes. Thyroid hormone further replaces the enhancer-bound NCoR-corepressor complex by the TRAP220 coactivator. Treatment with the HDAC inhibitor trichostatin A (TSA) causes activation of CAII transcription and histone H3 and H4 hyperacetylation at the enhancer, apparently without affecting binding of the two corepressor complexes. Unexpectedly, histone H3 and H4 at the fully repressed promoter are already hyperacetylated despite the close apposition of the MeCP2-targeted HDAC complex. Acetylation of histone H4, but not H3, at the promoter is moderately increased following TSA treatment. Our data suggest that the hyperacetylated but repressed CAII promoter is (partially) remodeled and primed for activation in v-ErbA-transformed cells.  (+info)

Induction of oligodendrocyte-like properties in a primitive hypothalamic cell line by cholesterol, an eye derived growth factor and brain extract. (8/207)

A serum-free medium has been devised which permits proliferation of the mouse primitive nervous cell line F7. When cholesterol, eye-derived growth factor and brain extract are added in this medium for 48 h, 80-90% of oligodendrocyte-like cells are generated. These cells have diminished substrate adhesion. They acquire the capacity to synthesize carbonic anhydrase II and myelin basic protein, two specific proteins of oligodendrocytes. These observations suggest that F7 clonal cell line, which has been previously shown to be a neurophysin cell precursor, is also a precursor for oligodendrocytes, and represents a bipotent stem cell line for both neuronal and glial cell lineages.  (+info)

Carbonic anhydrase II (CA-II) is a specific isoform of the carbonic anhydrase enzyme, which catalyzes the reversible reaction between carbon dioxide and water to form carbonic acid. This enzyme plays a crucial role in various physiological processes, including pH regulation, electrolyte balance, and biosynthetic reactions.

CA-II is widely distributed in the body, with high concentrations found in erythrocytes (red blood cells), the gastric mucosa, and renal tubules. In erythrocytes, CA-II facilitates the rapid conversion of carbon dioxide generated during cellular respiration to bicarbonate and protons, which can then be transported across the cell membrane for excretion or used in other metabolic processes.

In the gastric mucosa, CA-II helps regulate acid secretion by catalyzing the formation of carbonic acid from water and carbon dioxide, which subsequently dissociates into bicarbonate and a proton. The generated proton can then participate in the production of hydrochloric acid in the stomach.

In renal tubules, CA-II is involved in the reabsorption of bicarbonate ions from the filtrate back into the bloodstream, helping maintain electrolyte balance and pH homeostasis. Additionally, CA-II has been implicated in several pathological conditions, such as neurological disorders, cancer, and osteoporosis, making it a potential therapeutic target for drug development.

Carbonic anhydrases (CAs) are a group of enzymes that catalyze the reversible reaction between carbon dioxide and water to form carbonic acid, which then quickly dissociates into bicarbonate and a proton. This reaction is crucial for maintaining pH balance and regulating various physiological processes in the body, including respiration, secretion of electrolytes, and bone resorption.

There are several isoforms of carbonic anhydrases found in different tissues and organelles, each with distinct functions and properties. For example, CA I and II are primarily found in red blood cells, while CA III is present in various tissues such as the kidney, lung, and eye. CA IV is a membrane-bound enzyme that plays a role in transporting ions across cell membranes.

Carbonic anhydrases have been targeted for therapeutic interventions in several diseases, including glaucoma, epilepsy, and cancer. Inhibitors of carbonic anhydrases can reduce the production of bicarbonate and lower the pH of tumor cells, which may help to slow down their growth and proliferation. However, these inhibitors can also have side effects such as kidney stones and metabolic acidosis, so they must be used with caution.

Carbonic anhydrase inhibitors are a class of medications that work by blocking the action of carbonic anhydrase, an enzyme that is responsible for converting carbon dioxide and water into carbonic acid. This enzyme is found in various tissues throughout the body, including the eyes, kidneys, and nervous system.

By inhibiting the activity of carbonic anhydrase, these medications can reduce the production of bicarbonate ions in the body, which helps to lower the rate of fluid buildup in certain tissues. As a result, carbonic anhydrase inhibitors are often used to treat conditions such as glaucoma, epilepsy, and altitude sickness.

In glaucoma, for example, these medications can help to reduce pressure within the eye by promoting the drainage of fluid from the eye. In epilepsy, carbonic anhydrase inhibitors can help to reduce the frequency and severity of seizures by reducing the acidity of the blood and brain. And in altitude sickness, these medications can help to alleviate symptoms such as headache, nausea, and shortness of breath by reducing the buildup of fluid in the lungs.

Some common examples of carbonic anhydrase inhibitors include acetazolamide, methazolamide, and dorzolamide. These medications are available in various forms, including tablets, capsules, and eye drops, and are typically prescribed by a healthcare professional.

Carbonic anhydrase III (CAIII) is a member of the carbonic anhydrase enzyme family, which catalyzes the reversible reaction between carbon dioxide and water to form bicarbonate and protons. This enzyme is primarily found in muscle tissues, where it plays a role in regulating pH levels during muscle contraction and relaxation. CAIII has a lower catalytic activity compared to other carbonic anhydrase isoforms, suggesting that it may have additional functions beyond simple CO2 hydration. Additionally, CAIII has been implicated in various physiological processes such as protection against oxidative stress and regulation of muscle metabolism.

Ethoxzolamide is a carbonic anhydrase inhibitor drug that is primarily used to reduce fluid buildup in the eye (ocular pressure) caused by glaucoma or other conditions. It works by decreasing the production of fluid inside the eye, which helps lower the pressure within the eye.

Ethoxzolamide may also be used for other medical purposes, such as treating seizure disorders and preventing altitude sickness. The drug is available in oral tablet form and is typically taken 2-3 times a day.

It's important to note that Ethoxzolamide can have side effects, including frequent urination, tingling sensations in the hands or feet, loss of appetite, and changes in taste perception. It may also interact with other medications, so it's essential to inform your healthcare provider about all the drugs you are taking before starting Ethoxzolamide therapy.

Acetazolamide is a medication that belongs to a class of drugs called carbonic anhydrase inhibitors. It works by decreasing the production of bicarbonate in the body, which helps to reduce the amount of fluid in the eye and brain, making it useful for treating conditions such as glaucoma and epilepsy.

In medical terms, acetazolamide can be defined as: "A carbonic anhydrase inhibitor that is used to treat glaucoma, epilepsy, altitude sickness, and other conditions. It works by decreasing the production of bicarbonate in the body, which helps to reduce the amount of fluid in the eye and brain."

Acetazolamide may also be used for other purposes not listed here, so it is important to consult with a healthcare provider for specific medical advice.

Carbonic anhydrase I is a specific type of carbonic anhydrase, which is an enzyme that catalyzes the reversible reaction between carbon dioxide and water to form carbonic acid. This enzyme is primarily found in red blood cells and plays a crucial role in maintaining pH balance and regulating respiration.

Carbonic anhydrase I, also known as CA I or CA-I, is responsible for hydrating carbon dioxide to form bicarbonate ions and protons, which helps maintain the acid-base balance in the body. It has a relatively slower reaction rate compared to other carbonic anhydrase isoforms.

Defects or mutations in the CA I gene can lead to reduced enzymatic activity and may contribute to certain medical conditions, such as distal renal tubular acidosis (dRTA), a disorder characterized by impaired kidney function and acid-base imbalances. However, other carbonic anhydrase isoforms can compensate for the loss of CA I activity in most cases, so its deficiency rarely causes severe symptoms on its own.

Carbonic anhydrase IV (CA-IV), also known as membrane-associated carbonic anhydrase or CA-IX, is a member of the carbonic anhydrase enzyme family. This enzyme is responsible for catalyzing the reversible reaction that converts carbon dioxide and water into bicarbonate and a proton.

CA-IV is primarily found in the plasma membrane of polarized epithelial cells, where it plays a crucial role in maintaining acid-base balance and ion transport. It is also involved in various physiological processes, including respiration, bone resorption, and pH regulation.

Abnormalities in CA-IV expression or activity have been implicated in several diseases, such as cancer, kidney stones, and osteoporosis. In particular, overexpression of CA-IV has been observed in various types of cancer, where it contributes to tumor acidification, invasion, and metastasis. Therefore, CA-IV is considered a potential therapeutic target for cancer treatment.

Methazolamide is a sulfonamide-derived carbonic anhydrase inhibitor primarily used in the prevention and treatment of glaucoma. It works by decreasing the production of fluid inside the eye, which in turn lowers the pressure within the eye. Additionally, it has been used off-label for conditions such as altitude sickness, epilepsy, intracranial hypertension, and benign prostatic hyperplasia.

The medical definition of Methazolamide is:
A carbonic anhydrase inhibitor that reduces the secretion of aqueous humor, thereby lowering intraocular pressure; used in the treatment of glaucoma. It also has diuretic properties and has been used in the management of altitude sickness, epilepsy, intracranial hypertension, and benign prostatic hyperplasia.

Renal tubular acidosis (RTA) is a medical condition that occurs when the kidneys are unable to properly excrete acid into the urine, leading to an accumulation of acid in the bloodstream. This results in a state of metabolic acidosis.

There are several types of RTA, but renal tubular acidosis type 1 (also known as distal RTA) is characterized by a defect in the ability of the distal tubules to acidify the urine, leading to an inability to lower the pH of the urine below 5.5, even in the face of metabolic acidosis. This results in a persistently alkaline urine, which can lead to calcium phosphate stones and bone demineralization.

Type 1 RTA is often caused by inherited genetic defects, but it can also be acquired due to various kidney diseases, drugs, or autoimmune disorders. Symptoms of type 1 RTA may include fatigue, weakness, muscle cramps, decreased appetite, and vomiting. Treatment typically involves alkali therapy to correct the acidosis and prevent complications.

Osteopetrosis, also known as Albers-Schönberg disease or marble bone disease, is a group of rare genetic disorders characterized by increased bone density due to impaired bone resorption by osteoclasts. This results in brittle bones that are more susceptible to fractures and can also lead to various complications such as anemia, hearing loss, and vision problems. There are several types of osteopetrosis, which vary in severity and age of onset.

The medical definition of osteopetrosis is:

A genetic disorder characterized by defective bone resorption due to impaired osteoclast function, resulting in increased bone density, susceptibility to fractures, and potential complications such as anemia, hearing loss, and vision problems.

Bicarbonates, also known as sodium bicarbonate or baking soda, is a chemical compound with the formula NaHCO3. In the context of medical definitions, bicarbonates refer to the bicarbonate ion (HCO3-), which is an important buffer in the body that helps maintain normal pH levels in blood and other bodily fluids.

The balance of bicarbonate and carbonic acid in the body helps regulate the acidity or alkalinity of the blood, a condition known as pH balance. Bicarbonates are produced by the body and are also found in some foods and drinking water. They work to neutralize excess acid in the body and help maintain the normal pH range of 7.35 to 7.45.

In medical testing, bicarbonate levels may be measured as part of an electrolyte panel or as a component of arterial blood gas (ABG) analysis. Low bicarbonate levels can indicate metabolic acidosis, while high levels can indicate metabolic alkalosis. Both conditions can have serious consequences if not treated promptly and appropriately.

Benzolamide is not a recognized medication or pharmaceutical agent in modern medical practice. It is possible that you may have misspelled the name, and there are no direct synonyms for any known medications. If you meant to search for a different term or have more information about the context where this term was used, please let me know so I can provide a more accurate response.

Carbon dioxide (CO2) is a colorless, odorless gas that is naturally present in the Earth's atmosphere. It is a normal byproduct of cellular respiration in humans, animals, and plants, and is also produced through the combustion of fossil fuels such as coal, oil, and natural gas.

In medical terms, carbon dioxide is often used as a respiratory stimulant and to maintain the pH balance of blood. It is also used during certain medical procedures, such as laparoscopic surgery, to insufflate (inflate) the abdominal cavity and create a working space for the surgeon.

Elevated levels of carbon dioxide in the body can lead to respiratory acidosis, a condition characterized by an increased concentration of carbon dioxide in the blood and a decrease in pH. This can occur in conditions such as chronic obstructive pulmonary disease (COPD), asthma, or other lung diseases that impair breathing and gas exchange. Symptoms of respiratory acidosis may include shortness of breath, confusion, headache, and in severe cases, coma or death.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Dansyl compounds are fluorescent compounds that contain a dansyl group, which is a chemical group made up of a sulfonated derivative of dimethylaminonaphthalene. These compounds are often used as tracers in biochemical and medical research because they emit bright fluorescence when excited by ultraviolet or visible light. This property makes them useful for detecting and quantifying various biological molecules, such as amino acids, peptides, and proteins, in a variety of assays and techniques, including high-performance liquid chromatography (HPLC), thin-layer chromatography (TLC), and fluorescence microscopy.

The dansyl group can be attached to biological molecules through chemical reactions that involve the formation of covalent bonds between the sulfonate group in the dansyl compound and amino, thiol, or hydroxyl groups in the target molecule. The resulting dansylated molecules can then be detected and analyzed using various techniques.

Dansyl compounds are known for their high sensitivity, stability, and versatility, making them valuable tools in a wide range of research applications. However, it is important to note that the use of dansyl compounds requires careful handling and appropriate safety precautions, as they can be hazardous if mishandled or ingested.

Sodium-bicarbonate symporters, also known as sodium bicarbonate co-transporters, are membrane transport proteins that facilitate the movement of both sodium ions (Na+) and bicarbonate ions (HCO3-) across the cell membrane in the same direction. These transporters play a crucial role in maintaining acid-base balance in the body by regulating the concentration of bicarbonate ions, which is an important buffer in the blood and other bodily fluids.

The term "symporter" refers to the fact that these proteins transport two or more different molecules or ions in the same direction across a membrane. In this case, sodium-bicarbonate symporters co-transport one sodium ion and one bicarbonate ion together, usually using a concentration gradient of sodium to drive the uptake of bicarbonate.

These transporters are widely expressed in various tissues, including the kidneys, where they help reabsorb bicarbonate ions from the urine back into the bloodstream, and the gastrointestinal tract, where they contribute to the absorption of sodium and bicarbonate from food and drink. Dysfunction of sodium-bicarbonate symporters has been implicated in several diseases, including renal tubular acidosis and hypertension.

Zinc is an essential mineral that is vital for the functioning of over 300 enzymes and involved in various biological processes in the human body, including protein synthesis, DNA synthesis, immune function, wound healing, and cell division. It is a component of many proteins and participates in the maintenance of structural integrity and functionality of proteins. Zinc also plays a crucial role in maintaining the sense of taste and smell.

The recommended daily intake of zinc varies depending on age, sex, and life stage. Good dietary sources of zinc include red meat, poultry, seafood, beans, nuts, dairy products, and fortified cereals. Zinc deficiency can lead to various health problems, including impaired immune function, growth retardation, and developmental delays in children. On the other hand, excessive intake of zinc can also have adverse effects on health, such as nausea, vomiting, and impaired immune function.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Histidine is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H9N3O2. Histidine plays a crucial role in several physiological processes, including:

1. Protein synthesis: As an essential amino acid, histidine is required for the production of proteins, which are vital components of various tissues and organs in the body.

2. Hemoglobin synthesis: Histidine is a key component of hemoglobin, the protein in red blood cells responsible for carrying oxygen throughout the body. The imidazole side chain of histidine acts as a proton acceptor/donor, facilitating the release and uptake of oxygen by hemoglobin.

3. Acid-base balance: Histidine is involved in maintaining acid-base homeostasis through its role in the biosynthesis of histamine, which is a critical mediator of inflammatory responses and allergies. The decarboxylation of histidine results in the formation of histamine, which can increase vascular permeability and modulate immune responses.

4. Metal ion binding: Histidine has a high affinity for metal ions such as zinc, copper, and iron. This property allows histidine to participate in various enzymatic reactions and maintain the structural integrity of proteins.

5. Antioxidant defense: Histidine-containing dipeptides, like carnosine and anserine, have been shown to exhibit antioxidant properties by scavenging reactive oxygen species (ROS) and chelating metal ions. These compounds may contribute to the protection of proteins and DNA from oxidative damage.

Dietary sources of histidine include meat, poultry, fish, dairy products, and wheat germ. Histidine deficiency is rare but can lead to growth retardation, anemia, and impaired immune function.

In the context of medicine, particularly in relation to cancer treatment, protons refer to positively charged subatomic particles found in the nucleus of an atom. Proton therapy, a type of radiation therapy, uses a beam of protons to target and destroy cancer cells with high precision, minimizing damage to surrounding healthy tissue. The concentrated dose of radiation is delivered directly to the tumor site, reducing side effects and improving quality of life during treatment.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

Alcoholic pancreatitis is a specific type of pancreatitis, which is inflammation of the pancreas. This condition is caused by excessive and prolonged consumption of alcohol. The exact mechanism by which alcohol induces pancreatitis is not fully understood, but it is believed that alcohol causes damage to the cells of the pancreas, leading to inflammation. This can result in abdominal pain, nausea, vomiting, fever, and increased heart rate. Chronic alcoholic pancreatitis can also lead to serious complications such as diabetes, malnutrition, and pancreatic cancer. Treatment typically involves supportive care, such as hydration, pain management, and nutritional support, along with abstinence from alcohol. In severe cases, surgery may be necessary to remove damaged tissue or to relieve blockages in the pancreas.

Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.

Anion Exchange Protein 1, Erythrocyte (AE1), also known as Band 3 protein or SLC4A1, is a transmembrane protein found in the membranes of red blood cells (erythrocytes). It plays a crucial role in maintaining the pH and bicarbonate levels of the blood by facilitating the exchange of chloride ions (Cl-) with bicarbonate ions (HCO3-) between the red blood cells and the plasma.

The anion exchange protein 1 is composed of three major domains: a cytoplasmic domain, a transmembrane domain, and an extracellular domain. The cytoplasmic domain interacts with various proteins involved in regulating the cytoskeleton of the red blood cell, while the transmembrane domain contains the ion exchange site. The extracellular domain is responsible for the interaction between red blood cells and contributes to their aggregation.

Mutations in the AE1 gene can lead to various inherited disorders, such as hereditary spherocytosis, Southeast Asian ovalocytosis, and distal renal tubular acidosis type 1. These conditions are characterized by abnormal red blood cell shapes, impaired kidney function, or both.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

I apologize, but there seems to be no medical definition for "Carbonic Anhydrase V." Carbonic anhydrases are a family of enzymes that catalyze the reversible hydration of carbon dioxide to form bicarbonate and protons. There are several isoforms of carbonic anhydrase (CA I-IV, CA VI-VIII, etc.), but as far as current scientific knowledge and literature go, there isn't a recognized or well-established isoform called Carbonic Anhydrase V.

It is possible that you may have encountered a mistake or typographical error in your source material. If you have more context or information about where you found this term, I would be happy to help you further research the topic.

Sulfonamides are a group of synthetic antibacterial drugs that contain the sulfonamide group (SO2NH2) in their chemical structure. They are bacteriostatic agents, meaning they inhibit bacterial growth rather than killing them outright. Sulfonamides work by preventing the bacteria from synthesizing folic acid, which is essential for their survival.

The first sulfonamide drug was introduced in the 1930s and since then, many different sulfonamides have been developed with varying chemical structures and pharmacological properties. They are used to treat a wide range of bacterial infections, including urinary tract infections, respiratory tract infections, skin and soft tissue infections, and ear infections.

Some common sulfonamide drugs include sulfisoxazole, sulfamethoxazole, and trimethoprim-sulfamethoxazole (a combination of a sulfonamide and another antibiotic called trimethoprim). While sulfonamides are generally safe and effective when used as directed, they can cause side effects such as rash, nausea, and allergic reactions. It is important to follow the prescribing physician's instructions carefully and to report any unusual symptoms or side effects promptly.

Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.

Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.

Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.

Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.

Acrolein is an unsaturated aldehyde with the chemical formula CH2CHCHO. It is a colorless liquid that has a distinct unpleasant odor and is highly reactive. Acrolein is produced by the partial oxidation of certain organic compounds, such as glycerol and fatty acids, and it is also found in small amounts in some foods, such as coffee and bread.

Acrolein is a potent irritant to the eyes, nose, and throat, and exposure to high levels can cause coughing, wheezing, and shortness of breath. It has been shown to have toxic effects on the lungs, heart, and nervous system, and prolonged exposure has been linked to an increased risk of cancer.

In the medical field, acrolein is sometimes used as a laboratory reagent or as a preservative for biological specimens. However, due to its potential health hazards, it must be handled with care and appropriate safety precautions should be taken when working with this compound.

The oncogene proteins v-erbA are a subset of oncogenes that were initially discovered in retroviruses, specifically the avian erythroblastosis virus (AEV). These oncogenes are derived from normal cellular genes called proto-oncogenes, which play crucial roles in various cellular processes such as growth, differentiation, and survival.

The v-erbA oncogene protein is a truncated and mutated version of the thyroid hormone receptor alpha (THRA) gene, which is a nuclear receptor that regulates gene expression in response to thyroid hormones. The v-erbA protein can bind to DNA but cannot interact with thyroid hormones, leading to aberrant regulation of gene expression and uncontrolled cell growth, ultimately resulting in cancer.

In particular, the v-erbA oncogene has been implicated in the development of erythroblastosis, a disease characterized by the proliferation of immature red blood cells, leading to anemia and other symptoms. The activation of the v-erbA oncogene can also contribute to the development of other types of cancer, such as leukemia and lymphoma.

Medical definitions of water generally describe it as a colorless, odorless, tasteless liquid that is essential for all forms of life. It is a universal solvent, making it an excellent medium for transporting nutrients and waste products within the body. Water constitutes about 50-70% of an individual's body weight, depending on factors such as age, sex, and muscle mass.

In medical terms, water has several important functions in the human body:

1. Regulation of body temperature through perspiration and respiration.
2. Acting as a lubricant for joints and tissues.
3. Facilitating digestion by helping to break down food particles.
4. Transporting nutrients, oxygen, and waste products throughout the body.
5. Helping to maintain healthy skin and mucous membranes.
6. Assisting in the regulation of various bodily functions, such as blood pressure and heart rate.

Dehydration can occur when an individual does not consume enough water or loses too much fluid due to illness, exercise, or other factors. This can lead to a variety of symptoms, including dry mouth, fatigue, dizziness, and confusion. Severe dehydration can be life-threatening if left untreated.

Hydrogen bonding is not a medical term per se, but it is a fundamental concept in chemistry and biology that is relevant to the field of medicine. Here's a general definition:

Hydrogen bonding is a type of attractive force between molecules or within a molecule, which occurs when a hydrogen atom is bonded to a highly electronegative atom (like nitrogen, oxygen, or fluorine) and is then attracted to another electronegative atom. This attraction results in the formation of a partially covalent bond known as a "hydrogen bond."

In biological systems, hydrogen bonding plays a crucial role in the structure and function of many biomolecules, such as DNA, proteins, and carbohydrates. For example, the double helix structure of DNA is stabilized by hydrogen bonds between complementary base pairs (adenine-thymine and guanine-cytosine). Similarly, the three-dimensional structure of proteins is maintained by a network of hydrogen bonds that help to determine their function.

In medical contexts, hydrogen bonding can be relevant in understanding drug-receptor interactions, where hydrogen bonds between a drug molecule and its target protein can enhance the binding affinity and specificity of the interaction, leading to more effective therapeutic outcomes.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Antiporters, also known as exchange transporters, are a type of membrane transport protein that facilitate the exchange of two or more ions or molecules across a biological membrane in opposite directions. They allow for the movement of one type of ion or molecule into a cell while simultaneously moving another type out of the cell. This process is driven by the concentration gradient of one or both of the substances being transported. Antiporters play important roles in various physiological processes, including maintaining electrochemical balance and regulating pH levels within cells.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Carbonic anhydrase II (gene name CA2), is one of sixteen forms of human α carbonic anhydrases. Carbonic anhydrase catalyzes ... Sato S, Zhu XL, Sly WS (1990). "Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient ... Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. Loss of carbonic anhydrase ... Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annu. Rev. Biochem. 64 (1): 375-401. doi ...
carbonate dehydratase II. carbonic anhydrase B. carbonic anhydrase C. carbonic anhydrase II. carbonic dehydratase. cyanamide ... alpha_CA_I_II_III_XIII; Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc- ... Carbonic Anhydrases II and IX in Non-ampullary Duodenal Adenomas and Adenocarcinoma. Title: Carbonic Anhydrases II and IX in ... alpha_CA; Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze ...
Carbonic anhydrase 2 (human). Find diseases associated with this biological target and compounds tested against it in bioassay ...
CARBONIC ANHYDRASE II (human). Find diseases associated with this biological target and compounds tested against it in bioassay ...
Invitrogen Anti-Carbonic Anhydrase II Recombinant Monoclonal (ARC1451), Catalog # MA5-38188. Tested in Western Blot (WB) and ... carbonic anhydrase B; Carbonic anhydrase C; Carbonic anhydrase II; carbonic dehydratase; Cyanamide hydratase CA2; epididymis ... Carbonic Anhydrase II Antibody (MA5-38188) in WB Western blot analysis of Carbonic Anhydrase II in extracts of various cell ... Carbonic Anhydrase II Recombinant Rabbit Monoclonal Antibody (ARC1451). View all (50) Carbonic Anhydrase II antibodies ...
Crystal structure of human carbonic anhydrase isozyme II with 5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide ... Crystal structure of human carbonic anhydrase isozyme II with 5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide. *PDB ... Crystal structure of human carbonic anhydrase isozyme II with 5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide. ... Carbonic anhydrase 2. A. 260. Homo sapiens. Mutation(s): 0 Gene Names: CA2. EC: (PDB Primary Data), (UniProt) ...
Carbonic anhydrase is used to create carbon dioxide capture systems and to research various purification techniques ; Carbonic ... Carbonic Anhydrase II bovine (≥ 90% SDS-PAGE, Escherichia coli, main ≥ 5,000units/mg protein, buffered aqueous solution); ... Carbonic anhydrase is also used to study acid-base regulation in fish and carbonic anhydrase type II deficiency syndrome . ... Lack of carbonic anhydrase results in carbonic anhydrase type II deficiency syndrome, which is an autosomal recessive disease ...
... the carbonic anhydrase II gene, and KS sulfation in the embryonic chicken cornea. Download Prime PubMed App to iPhone, iPad, or ... AnimalsCarbonic Anhydrase IIChick EmbryoChondroitin Sulfate ProteoglycansCorneaCrystallinsEmbryonic DevelopmentGene Expression ... TY - JOUR T1 - Thyroxine affects expression of KSPG-related genes, the carbonic anhydrase II gene, and KS sulfation in the ... Thyroxine affects expression of KSPG-related genes, the carbonic anhydrase II gene, and KS sulfation in the embryonic chicken ...
Thermodynamic, Kinetic and Crystallographic Investigations of Benzenesulfonamides as Ligands of Human Carbonic Anhydrase II The ... Kinetic and Structural Characterization of Inhibitor Binding to Aldose Reductase and Carbonic Anhydrase II by: Rechlin, Chris ...
Screening Derivatized Peptide Libraries for Tight Binding Inhibitors to Carbonic Anhydrase II by Electrospray Ionization-Mass ... to screen two libraries of soluble compounds to search for tight binding inhibitors for carbonic anhydrase II (EC The ... Screening Derivatized Peptide Libraries for Tight Binding Inhibitors to Carbonic Anhydrase II by Electrospray Ionization-Mass ... Tight Binding InhibitorscompoundacidECAA 2AA 1CHCarbonic Anhydrase IIScreening Derivatized Peptide LibrariesSCinhibitorbinding ...
17b -estradiol suppresses gene expression of tartrate resistant acid phosphatase and carbonic anhydrase II in ovariectomized ... 17b -estradiol suppresses gene expression of tartrate resistant acid phosphatase and carbonic anhydrase II in ovariectomized ... title = "17b -estradiol suppresses gene expression of tartrate resistant acid phosphatase and carbonic anhydrase II in ... 17b -estradiol suppresses gene expression of tartrate resistant acid phosphatase and carbonic anhydrase II in ovariectomized ...
Carbonic anhydrase 22-(N-MORPHOLINO)-ETHANESULFONIC ACID2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl] ... 2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide (Link to PubChem not yet available). ...
More than 100 distinct human carbonic anhydrase II (HCAII) 3D structures have been generated in last 3 decades [Liljas A, et al ... CARBONIC ANHYDRASE 2. A [auth X]. 260. Homo sapiens. Mutation(s): 0 Gene Names: CA2. EC: (PDB Primary Data), ( ... Structural Study of X-Ray Induced Activation of Carbonic Anhydrase.. Sjoblom, B., Polentarutti, M., Djinovic-Carugo, K.. (2009 ... Carbonic anhydrase, a zinc metalloenzyme, catalyzes the reversible hydration of carbon dioxide to bicarbonate. It is involved ...
Dual carbonic anhydrase and cyclooxygenase-2 inhibition. / Dogné, Jean-Michel; Thiry, Anne; Masereel, Bernard et al. Drug ... Dogné J-M, Thiry A, Masereel B, Supuran C. Dual carbonic anhydrase and cyclooxygenase-2 inhibition. In Claudiu T, Jean-Yves S, ... Dogné, J-M, Thiry, A, Masereel, B & Supuran, C 2009, Dual carbonic anhydrase and cyclooxygenase-2 inhibition. in T Claudiu & S ... Dogné, J-M., Thiry, A., Masereel, B., & Supuran, C. (2009). Dual carbonic anhydrase and cyclooxygenase-2 inhibition. In T. ...
... is a highly pure recombinant protein developed by Assay Genie for use ... Carbonic anhydrase II is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with ... Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to ... Carbonic Anhydrase II/CA2 Recombinant Protein The carbonic anhydrases (or carbonate dehydratases) are classified as ...
Osteopetrosis in carbonic anhydrase isoenzyme II deficiency. A distinct form of osteopetrosis occurs in association with renal ... The specific genetic defect in humans with osteopetrosis is caused by carbonic anhydrase II deficiency (discussed below) ... occurs in association with renal tubular acidosis and cerebral calcification due to carbonic anhydrase isoenzyme II deficiency ... tubular acidosis and cerebral calcification due to carbonic anhydrase isoenzyme II deficiency. This enzyme catalyzes the ...
Proton Transfer From HIS200 in Human Carbonic Anhydrase II ... Proton Transfer From HIS200 in Human Carbonic Anhydrase II. ... The structure of Proton Transfer From HIS200 in Human Carbonic Anhydrase II, PDB code: 1yo2 was solved by D.Bhatt, C.Tu, S.Z. ... Zinc binding site 1 out of 1 in the Proton Transfer From HIS200 in Human Carbonic Anhydrase II. Mono view Stereo pair view ... The binding sites of Zinc atom in the Proton Transfer From HIS200 in Human Carbonic Anhydrase II (pdb code 1yo2). This binding ...
Carbonic anhydrase II deficiency syndrome with amelogenesis imperfecta linked to a homozygous CA2 deletion. Leite LDR, Resende ... a study to present a phenotypic and genotypic characterization of a patient clinically diagnosed with carbonic anhydrase II ( ...
Using a 96-well plate assay, oestrone-3-O-sulphamate (EMATE) and two coumarin-based sulphamate drugs (667 COUMATE and STX 118) ... Carbonic anhydrases (CAs) are expressed by many solid tumours where they may act to confer a growth advantage on malignant ... Antineoplastic Agents, Binding Sites, Carbonic Anhydrase II, Carbonic Anhydrase Inhibitors, Estrone, Humans, Inhibitory ... Inhibition of carbonic anhydrase II by steroidal and non-steroidal sulphamates. Ho YT., Purohit A., Vicker N., Newman SP., ...
Behnke, C.A. et al., Atomic resolution studies of carbonic anhydrase II. Acta Crystallogr.,Sect.D (2010) Release Date. 2003-09- ... Full Matrix Error Analysis of Carbonic Anhydrase Coordinates. PDB Format Method. X-RAY DIFFRACTION 0.95 Å. Oligo State. monomer ... 1 x HG: MERCURY (II) ION(Non-covalent). HG.2: 2 residues within 4Å:*. Chain A: F.129 ... 2 x GOL: GLYCEROL(Non-functional Binders). GOL.5: 10 residues within 4Å:*. Chain A: N.61, H.63, A.64, N.66, Q.91, H.93, H.95, T ...
Carbonic Anhydrase II Complexed With (S)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide ... Carbonic Anhydrase II Complexed With (S)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide Coordinates. PDB Format Method ... 1 x HG: MERCURY (II) ION(Non-covalent). HG.2: 4 residues within 4Å:*. Chain A: V.133, Q.135, E.203, C.204 ... 1 x SBS: (S)-N-(3-INDOL-1-YL-2-METHYL-PROPYL)-4-SULFAMOYL-BENZAMIDE(Non-covalent). SBS.3: 13 residues within 4Å:*. Chain A: H. ...
... the severity of which may be asymmetric in the two eyes. This article reviews glaucoma associated with increased episcleral v ... Carbonic anhydrase inhibitors. Class Summary. Enzyme found in many tissues of the body, including the eye. Catalyzes a ... Medications used to decrease aqueous production include beta-blockers (topical), carbonic anhydrase inhibitors (topical and/or ... Catalyzes reversible reaction involving hydration of carbon dioxide and dehydration of carbonic acid. May use concomitantly ...
Identification and Measurement of Carbonic Anhydrase-II Molecule Numbers in the Rat Carotid Body ... Identification and Measurement of Carbonic Anhydrase-II Molecule Numbers in the Rat Carotid Body Guglielmo Di Tano1, Claudia ... Carbonic anhydrase (CA) in the carotid body (CB) plays an important role in the maintenance of blood PO2 and PCO2/pH ... This value corresponds to 4.57 ng CA-II. When compared with a rat CA-II calibration curve, an average of number of 3.54 x 107 ...
Primary Duodenal Adenocarcinoma Expressing Carbonic Anhydrase IX. Primary Duodenal Adenocarcinoma Expressing Carbonic Anhydrase ... Primary duodenal adenocarcinoma is a rare malignancy whose carbonic anhydrase IX (CA9) expression remains poorly understood. A ...
The carbonic anhydrase I (CA I) inhibition of copper(II) complexes which goes on competitively was determined by using UV-Vis ... Copper(II) sulfonamide complexes having enzyme inhibition activities on carbonic anhydrase I: synthesis, characterization and ... Carbonic anhydrase I, Enzyme inhibition, Voltammetry, ELECTROCHEMICAL INVESTIGATIONS, AMPEROMETRIC DETERMINATION, ISOZYME-II, ... In general, sulfonamides and their derivatives are researched for their inhibitory effects on carbonic anhydrase isoenzymes ( ...
Carbonic Anhydrase XIV (cluster #2 Of 8), Eukaryotic (5 Compounds) Code:. CAH14-2-E. Compound Summary. Annotation Type. ... Carbonic Anhydrase XIV (cluster #1 Of 8), Eukaryotic. 185. 44. 16. 21. ... Carbonic Anhydrase XIV (cluster #3 Of 8), Eukaryotic. 1. 1. 0. 0. ... Carbonic Anhydrase XIV (cluster #4 Of 8), Eukaryotic. 57. 24. 15. 12. ...
Carbonic Anhydrase II as Target for Drug Design (271 views). Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 51-90.. ... Carbonic Anhydrase VII (226 views). Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 151-168.. Impact Factor: 0. View ... Carbonic Anhydrases: An Overview (285 views). Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 3-13.. Impact Factor: 0. ... Human Carbonic Anhydrases: Catalytic Properties, Structural Features, and Tissue Distribution (325 views). Carbonic Anhydrases ...

No FAQ available that match "carbonic anhydrase ii"

No images available that match "carbonic anhydrase ii"