Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
The 4-aminomethyl form of VITAMIN B 6. During transamination of amino acids, PYRIDOXAL PHOSPHATE is transiently converted into pyridoxamine phosphate.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.
An enzyme that catalyzes the conversion of L-TYROSINE and 2-oxoglutarate to 4-hydroxyphenylpyruvate and L-GLUTAMATE. It is a pyridoxal-phosphate protein. L-PHENYLALANINE is hydroxylated to L-tyrosine. The mitochondrial enzyme may be identical with ASPARTATE AMINOTRANSFERASES (EC 2.6.1.1.). Deficiency of this enzyme may cause type II Tyrosinemia (see TYROSINEMIAS). EC 2.6.1.5.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (From Enzyme Nomenclature, 1992) EC 2.1.3.2.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
A set of opposing, nonequilibrium reactions catalyzed by different enzymes which act simultaneously, with at least one of the reactions driven by ATP hydrolysis. The results of the cycle are that ATP energy is depleted, heat is produced and no net substrate-to-product conversion is achieved. Examples of substrate cycling are cycling of gluconeogenesis and glycolysis pathways and cycling of the triglycerides and fatty acid pathways. Rates of substrate cycling may be increased many-fold in association with hypermetabolic states resulting from severe burns, cold exposure, hyperthyroidism, or acute exercise.
A group of compounds that are derivatives of phenylpyruvic acid which has the general formula C6H5CH2COCOOH, and is a metabolite of phenylalanine. (From Dorland, 28th ed)
A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer amino group from L-TRYPTOPHAN to 2-oxoglutarate in order to generate indolepyruvate and L-GLUTAMATE.
A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transamination of branched-chain AMINO ACIDS to 2-oxoglutarate.
A pyridoxal-phosphate protein that catalyzes the conversion of L-tyrosine to tyramine and carbon dioxide. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. (From Enzyme Nomenclature, 1992) EC 4.1.1.25.
Glyoxylates are organic compounds that are intermediate products in the metabolic pathways responsible for the breakdown and synthesis of various molecules, including amino acids and carbohydrates, and are involved in several biochemical processes such as the glyoxylate cycle.
A broad-spectrum excitatory amino acid antagonist used as a research tool.
An enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.
Amino acids which have a branched carbon chain.
Blood tests that are used to evaluate how well a patient's liver is working and also to help diagnose liver conditions.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Activities of citrate synthase, NAD+-linked and NADP+-linked isocitrate dehydrogenases, glutamate dehydrogenase, aspartate aminotransferase and alanine aminotransferase in nervous tissues from vertebrates and invertebrates. (1/2887)

1. The activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenases were measured in nervous tissue from different animals in an attempt to provide more information about the citric acid cycle in this tissue. In higher animals the activities of citrate synthase are greater than the sum of activities of the isocitrate dehydrogenases, whereas they are similar in nervous tissues from the lower animals. This suggests that in higher animals the isocitrate dehydrogenase reaction is far-removed from equilibrium. If it is assumed that isocitrate dehydrogenase activities provide an indication of the maximum flux through the citric acid cycle, the maximum glycolytic capacity in nervous tissue is considerably greater than that of the cycle. This suggest that glycolysis can provide energy in excess of the aerobic capacity of the tissue. 2. The activities of glutamate dehydrogenase are high in most nervous tissues and the activities of aspartate aminotransferase are high in all nervous tissue investigated. However, the activities of alanine aminotransferase are low in all tissues except the ganglia of the waterbug and cockroach. In these insect tissues, anaerobic glycolysis may result in the formation of alanine rather than lactate.  (+info)

Blockade of type beta transforming growth factor signaling prevents liver fibrosis and dysfunction in the rat. (2/2887)

We eliminated type beta transforming growth factor (TGF-beta) signaling by adenovirus-mediated local expression of a dominant-negative type II TGF-beta receptor (AdCATbeta-TR) in the liver of rats treated with dimethylnitrosamine, a model of persistent liver fibrosis. In rats that received a single application of AdCATbeta-TR via the portal vein, liver fibrosis as assessed by histology and hydroxyproline content was markedly attenuated. All AdCATbeta-TR-treated rats remained alive, and their serum levels of hyaluronic acid and transaminases remained at low levels, whereas all the AdCATbeta-TR-untreated rats died of liver dysfunction. The results demonstrate that TGF-beta does play a central role in liver fibrogenesis and indicate clearly in a persistent fibrosis model that prevention of fibrosis by anti-TGF-beta intervention could be therapeutically useful.  (+info)

Enrichment of canalicular membrane with cholesterol and sphingomyelin prevents bile salt-induced hepatic damage. (3/2887)

These studies were undertaken to characterize the role of plasma membrane cholesterol in canalicular secretory functions and hepatocyte integrity against intravenous taurocholate administration. Cholesterol and sphingomyelin concentrations and cholesterol/phospholipid ratios were significantly increased in canalicular membranes of diosgenin-fed rats, suggesting a more resistant structure against solubilization by taurocholate. During taurocholate infusion, control rats had significantly decreased bile flow, whereas diosgenin-fed animals maintained bile flow. Maximal cholesterol output increased by 176% in diosgenin-fed rats, suggesting an increased precursor pool of biliary cholesterol in these animals. Maximal phospholipid output only increased by 43% in diosgenin-fed rats, whereas bile salt output remained at control levels. The kinetics of glutamic oxalacetic transaminase, lactic dehydrogenase, and alkaline phosphatase activities in bile showed a significantly faster release in control than in diosgenin-fed rats. After 30 min of intravenous taurocholate infusion, necrotic hepatocytes were significantly increased in control animals. Preservation of bile secretory functions and hepatocellular cytoprotection by diosgenin against the intravenous infusion of toxic doses of taurocholate was associated with an increased concentration of cholesterol and sphingomyelin in the canalicular membrane. The increase of biliary cholesterol output induced by diosgenin was correlated to the enhanced concentration of cholesterol in the canalicular membrane.  (+info)

Phase I and pharmacokinetic study of the topoisomerase II catalytic inhibitor fostriecin. (4/2887)

We conducted a phase I and pharmacokinetic study of the topoisomerase II catalytic inhibitor fostriecin. Fostriecin was administered intravenously over 60 min on days 1-5 at 4-week intervals. Dose was escalated from 2 mg m(-2) day(-1) to 20 mg m(-2) day(-1) in 20 patients. Drug pharmacokinetics was analysed with high performance liquid chromatography with UV-detection. Plasma collected during drug administration was tested in vitro for growth inhibition of a teniposide-resistant small-cell lung cancer (SCLC) cell line. The predominant toxicities were elevated liver transaminases (maximum common toxicity criteria (CTC) grade 4) and serum creatinine (maximum CTC grade 2). These showed only a limited increase with increasing doses, often recovered during drug administration and were fully reversible. Duration of elevated alanine-amino transferase (ALT) was dose-limiting in one patient at 20 mg m(-2). Other frequent toxicities were grade 1-2 nausea/vomiting, fever and mild fatigue. Mean fostriecin plasma half-life was 0.36 h (initial; 95% CI, 0-0.76 h) and 1.51 h (terminal; 95% CI, 0.41-2.61 h). A metabolite, most probably dephosphorylated fostriecin, was detected in plasma and urine. No tumour responses were observed, but the plasma concentrations reached in the patients were insufficient to induce significant growth inhibition in vitro. The maximum tolerated dose (MTD) has not been reached, because drug supply was stopped at the 20 mg m(-2) dose level. However, further escalation seems possible and is warranted to achieve potentially effective drug levels. Fostriecin has a short plasma half-life and longer duration of infusion should be considered.  (+info)

Influences of Kupffer cell stimulation and suppression on immunological liver injury in mice. (5/2887)

AIM: To study the possible involvement of Kupffer cells (KC) in immunological liver injury in mice. METHODS: Liver injury was induced by i.v. injection of Bacillus Calmette-Guerin (BCG) 5 x 10(7) viable bacilli followed by i.v. injection of lipopolysaccharides (LPS) 7.5 micrograms to each mouse. Indian ink and silica were i.v. injected to suppress KC and retinol was given po to stimulate KC in these mice. Plasma alanine aminotransferase (AlaAT), aspatate aminotransferase (AspAT), nitric oxide (NO), and liver tissue were examined. RESULTS: Injection of LPS following BCG injection resulted in a remarkable elevation of plasma NO, AlaAT, and AspAT levels, and severe liver damage. The damages were enhanced by the activation of KC with retinol and reduced by suppression of KC with silica and Indian ink. CONCLUSION: The degree of liver injury induced by BCG + LPS is closely correlated with the status of KC, and NO from KC plays an important role in the pathogenesis of the liver damage in mice.  (+info)

Effect of epidermal growth factor on cultured rat hepatocytes poisoned by CCl4. (6/2887)

AIM: To study the effects of epidermal growth factor (EGF) on CCl4-induced primary cultured hepatocytes injury. METHODS: Alanine amino-transferase (AlaAT) and aspartate aminotransferase (AspAT) activities and K+ concentractions were determined by the Auto-biochemistry Assay System. Malondialdehyde (MDA) was determined by thiobarbituric acid method. Radioactivity was determined by liquid scintillometry. Light microscopy and electron microscopy were used. RESULTS: EGF 40 micrograms.L-1 decreased CCl4 (10 mmol.L-1)-induced damages of rat primary cultured hepatocytes by decreasing AlaAT and AspAT leakage and MDA production, and promoted RNA and DNA synthesis, with a high positive correlation between intracellular K+ leakage and DNA syntheses (r = 0.99, P < 0.01). Cytopathological study showed that EGF decreased damage of liver cells. CONCLUSION: EGF maintains the stability of cellular lipid membrane and promotes syntheses of RNA and DNA of hepatocytes, and intracellular K+ transference is a promotor of the message transmission of DNA synthesis.  (+info)

Opposite behavior of two isozymes when refolding in the presence of non-ionic detergents. (7/2887)

GroEL has a greater affinity for the mitochondrial isozyme (mAAT) of aspartate aminotransferase than for its cytosolic counterpart (cAAT) (Mattingly JR Jr, Iriarte A, Martinez-Carrion M, 1995, J Biol Chem 270:1138-1148), two proteins that share a high degree of sequence similarity and an almost identical spatial structure. The effect of detergents on the refolding of these large, dimeric isozymes parallels this difference in behavior. The presence of non-ionic detergents such as Triton X-100 or lubrol at concentrations above their critical micelle concentration (CMC) interferes with reactivation of mAAT unfolded in guanidinium chloride but increases the yield of cAAT refolding at low temperatures. The inhibitory effect of detergents on the reactivation of mAAT decreases progressively as the addition of detergents is delayed after starting the refolding reaction. The rate of disappearance of the species with affinity for binding detergents coincides with the slowest of the two rate-limiting steps detected in the refolding pathway of mAAT. Limited proteolysis studies indicate that the overall structure of the detergent-bound mAAT resembles that of the protein in a complex with GroEL. The mAAT folding intermediates trapped in the presence of detergents can resume reactivation either upon dilution of the detergent below its CMC or by adding beta-cyclodextrin. Thus, isolation of otherwise transient productive folding intermediates for further characterization is possible through the use of detergents.  (+info)

Folate nutriture alters choline status of women and men fed low choline diets. (8/2887)

Choline and folate share methylation pathways and, in studies of rats, were shown to be metabolically inter-related. To determine whether choline status is related to folate intake in humans, we measured the effect of controlled folate depletion and repletion on the plasma choline and phosphatidylcholine concentrations of 11 healthy men (33-46 y) and 10 healthy women (49-63 y) fed low-choline diets in two separate metabolic unit studies. Total folate intake was varied by supplementing low folate (25 and 56 microg/d for men and women, respectively) and low choline (238 and 147 mg/d for men and women, respectively) diets with pteroylglutamic acid for 2-6 wk following folate-depletion periods of 4-5 wk. The low folate/choline intakes resulted in subclinical folate deficiencies; mean plasma choline decreases of 28 and 25% in the men and women, respectively; and a plasma phosphatidylcholine decrease of 26% in the men (P < 0. 05). No functional choline deficiency occurred, as measured by serum transaminase and lipid concentrations. The decreases in choline status measures returned to baseline or higher upon moderate folate repletion and were more responsive to folate repletion than plasma folate and homocysteine. Feeding methionine supplements to the men did not prevent plasma choline depletion, indicating that folate is a more limiting nutrient for these methylation pathways. The results indicate that 1) choline is utilized as a methyl donor when folate intake is low, 2) the de novo synthesis of phosphatidylcholine is insufficient to maintain choline status when intakes of folate and choline are low, and 3) dietary choline is required by adults in an amount > 250 mg/d to maintain plasma choline and phosphatidylcholine when folate intake is low.  (+info)

Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.

In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.

It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.

Pyridoxamine is a form of vitamin B6, which is a water-soluble vitamin that plays an essential role in the body's protein metabolism, neurotransmitter synthesis, and hemoglobin production. Pyridoxamine is a specific chemical compound that is a derivative of pyridoxine, another form of vitamin B6.

Pyridoxamine functions as a cofactor for various enzymes involved in the metabolism of amino acids, the building blocks of proteins. It helps to convert harmful homocysteine into the essential amino acid methionine, which is important for maintaining normal levels of homocysteine and supporting cardiovascular health.

Pyridoxamine has been studied for its potential role in treating or preventing certain medical conditions, such as diabetic nephropathy and neurodegenerative diseases, due to its antioxidant properties and ability to protect against protein glycation, a process that can damage tissues and contribute to aging and disease. However, more research is needed to establish its safety and efficacy for these uses.

Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.

There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.

Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Alanine transaminase (ALT) is a type of enzyme found primarily in the cells of the liver and, to a lesser extent, in the cells of other tissues such as the heart, muscles, and kidneys. Its primary function is to catalyze the reversible transfer of an amino group from alanine to another alpha-keto acid, usually pyruvate, to form pyruvate and another amino acid, usually glutamate. This process is known as the transamination reaction.

When liver cells are damaged or destroyed due to various reasons such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, or drug-induced liver injury, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood is a useful diagnostic tool for evaluating liver function and detecting liver damage. Normal ALT levels vary depending on the laboratory, but typically range from 7 to 56 units per liter (U/L) for men and 6 to 45 U/L for women. Elevated ALT levels may indicate liver injury or disease, although other factors such as muscle damage or heart disease can also cause elevations in ALT.

Tyrosine transaminase, also known as tyrosine aminotransferase or TAT, is an enzyme that plays a crucial role in the metabolism of the amino acid tyrosine. This enzyme catalyzes the transfer of an amino group from tyrosine to a ketoacid, such as alpha-ketoglutarate, resulting in the formation of a new amino acid, glutamate, and a ketone derivative of tyrosine.

Tyrosine transaminase is primarily found in the liver and its activity can be used as a biomarker for liver function. Increased levels of this enzyme in the blood may indicate liver damage or disease, such as hepatitis or cirrhosis. Therefore, measuring tyrosine transaminase activity is often part of routine liver function tests.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Aspartate carbamoyltransferase (ACT) is a crucial enzyme in the urea cycle, which is the biochemical pathway responsible for the elimination of excess nitrogen waste from the body. This enzyme catalyzes the second step of the urea cycle, where it facilitates the transfer of a carbamoyl group from carbamoyl phosphate to aspartic acid, forming N-acetylglutamic semialdehyde and releasing phosphate in the process.

The reaction catalyzed by aspartate carbamoyltransferase is as follows:

Carbamoyl phosphate + L-aspartate → N-acetylglutamic semialdehyde + P\_i + CO\_2

This enzyme plays a critical role in maintaining nitrogen balance and preventing the accumulation of toxic levels of ammonia in the body. Deficiencies or mutations in aspartate carbamoyltransferase can lead to serious metabolic disorders, such as citrullinemia and hyperammonemia, which can have severe neurological consequences if left untreated.

Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CO2H. It is one of the twenty standard amino acids, and it is a polar, negatively charged, and hydrophilic amino acid. In proteins, aspartic acid usually occurs in its ionized form, aspartate, which has a single negative charge.

Aspartic acid plays important roles in various biological processes, including metabolism, neurotransmitter synthesis, and energy production. It is also a key component of many enzymes and proteins, where it often contributes to the formation of ionic bonds and helps stabilize protein structure.

In addition to its role as a building block of proteins, aspartic acid is also used in the synthesis of other important biological molecules, such as nucleotides, which are the building blocks of DNA and RNA. It is also a component of the dipeptide aspartame, an artificial sweetener that is widely used in food and beverages.

Like other amino acids, aspartic acid is essential for human health, but it cannot be synthesized by the body and must be obtained through the diet. Foods that are rich in aspartic acid include meat, poultry, fish, dairy products, eggs, legumes, and some fruits and vegetables.

Substrate cycling, also known as futile cycling, refers to a metabolic process in which there is a repeated conversion of a substrate to a product and then back to the original substrate, often consuming energy in the form of ATP without any net physiological benefit. This process can occur under certain pathophysiological conditions or as a result of genetic mutations affecting enzyme regulation. The most well-known example is the Cori cycle, where lactate produced by muscles is converted back to glucose in the liver, only to be released again and used by the muscles.

Phenylpyruvic acid is not a medical condition, but rather a chemical compound that is produced in the body. It is a byproduct of phenylalanine metabolism, an essential amino acid that cannot be synthesized by the human body and must be obtained through dietary sources such as proteins.

In some rare genetic disorders, such as phenylketonuria (PKU), the body is unable to properly metabolize phenylalanine due to a deficiency or malfunction of the enzyme phenylalanine hydroxylase. As a result, phenylpyruvic acid and other toxic byproducts accumulate in the body, leading to various health problems such as intellectual disability, seizures, and behavioral issues.

Therefore, the medical relevance of phenylpyruvic acid lies in its association with certain metabolic disorders, particularly PKU, and its potential use as a diagnostic marker for these conditions.

Tryptophan transaminase, also known as tryptophan aminotransferase or L-tryptophan aminotransferase, is an enzyme involved in the metabolism of the essential amino acid tryptophan. This enzyme catalyzes the transfer of an amino group from tryptophan to a ketoacid acceptor, such as alpha-ketoglutarate, resulting in the formation of beta-amino-isocaproic acid and glutamate. The reaction is part of the larger catabolic pathway for tryptophan degradation, which eventually leads to the production of several biologically important compounds, including niacin (vitamin B3) and serotonin, a neurotransmitter.

Tryptophan transaminase plays a crucial role in maintaining the balance of amino acids in the body and ensuring their proper utilization for various physiological functions. Dysregulation or deficiency of this enzyme can contribute to several metabolic disorders, including hyperphenylalaninemia (elevated levels of phenylalanine) and certain neurological conditions due to impaired serotonin synthesis.

Leucine transaminase, also known as Alanine transaminase (ALT) or Serum glutamate-pyruvate transaminase (SGPT), is an enzyme found primarily in the liver but also in smaller amounts in other tissues such as the heart, muscles, and kidneys. It plays a role in the metabolism of amino acids.

When liver cells are damaged or destroyed, such as in cases of hepatitis, liver damage, or liver disease, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood can be used as a diagnostic tool to help detect and monitor liver injury or disease. However, it's important to note that other factors can also affect ALT levels, so results must be interpreted in conjunction with other clinical findings and tests.

Tyrosine decarboxylase is an enzyme that catalyzes the decarboxylation of the amino acid tyrosine to form the biogenic amine tyramine. The reaction occurs in the absence of molecular oxygen and requires pyridoxal phosphate as a cofactor. Tyrosine decarboxylase is found in various bacteria, fungi, and plants, and it plays a role in the biosynthesis of alkaloids and other natural products. In humans, tyrosine decarboxylase is not normally present, but its activity has been detected in some tumors and is associated with the production of neurotransmitters in neuronal cells.

Glyoxylates are organic compounds that are intermediates in various metabolic pathways, including the glyoxylate cycle. The glyoxylate cycle is a modified version of the Krebs cycle (also known as the citric acid cycle) and is found in plants, bacteria, and some fungi.

Glyoxylates are formed from the breakdown of certain amino acids or from the oxidation of one-carbon units. They can be converted into glycine, an important amino acid involved in various metabolic processes. In the glyoxylate cycle, glyoxylates are combined with acetyl-CoA to form malate and succinate, which can then be used to synthesize glucose or other organic compounds.

Abnormal accumulation of glyoxylates in the body can lead to the formation of calcium oxalate crystals, which can cause kidney stones and other health problems. Certain genetic disorders, such as primary hyperoxaluria, can result in overproduction of glyoxylates and increased risk of kidney stone formation.

Kynurenic acid is a metabolite of the amino acid tryptophan, which is formed through the kynurenine pathway. It functions as an antagonist at glutamate receptors and acts as a neuroprotective agent by blocking excessive stimulation of NMDA receptors in the brain. Additionally, kynurenic acid also has anti-inflammatory properties and is involved in the regulation of the immune response. Abnormal levels of kynurenic acid have been implicated in several neurological disorders such as schizophrenia, epilepsy, and Huntington's disease.

4-Aminobutyrate transaminase (GABA transaminase or GABA-T) is an enzyme that catalyzes the reversible transfer of an amino group from 4-aminobutyrate (GABA) to 2-oxoglutarate, forming succinic semialdehyde and glutamate. This enzyme plays a crucial role in the metabolism of the major inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the central nervous system. Inhibition of GABA transaminase is a therapeutic strategy for the treatment of various neurological disorders, such as epilepsy and anxiety, due to its ability to increase GABA levels in the brain.

Branched-chain amino acids (BCAAs) are a group of three essential amino acids: leucine, isoleucine, and valine. They are called "branched-chain" because of their chemical structure, which has a side chain that branches off from the main part of the molecule.

BCAAs are essential because they cannot be produced by the human body and must be obtained through diet or supplementation. They are crucial for muscle growth and repair, and play a role in energy production during exercise. BCAAs are also important for maintaining proper immune function and can help to reduce muscle soreness and fatigue after exercise.

Foods that are good sources of BCAAs include meat, poultry, fish, eggs, dairy products, and legumes. BCAAs are also available as dietary supplements, which are often used by athletes and bodybuilders to enhance muscle growth and recovery. However, it is important to note that excessive intake of BCAAs may have adverse effects on liver function and insulin sensitivity, so it is recommended to consult with a healthcare provider before starting any new supplement regimen.

Liver function tests (LFTs) are a group of blood tests that are used to assess the functioning and health of the liver. These tests measure the levels of various enzymes, proteins, and waste products that are produced or metabolized by the liver. Some common LFTs include:

1. Alanine aminotransferase (ALT): An enzyme found primarily in the liver, ALT is released into the bloodstream in response to liver cell damage. Elevated levels of ALT may indicate liver injury or disease.
2. Aspartate aminotransferase (AST): Another enzyme found in various tissues, including the liver, heart, and muscles. Like ALT, AST is released into the bloodstream following tissue damage. High AST levels can be a sign of liver damage or other medical conditions.
3. Alkaline phosphatase (ALP): An enzyme found in several organs, including the liver, bile ducts, and bones. Elevated ALP levels may indicate a blockage in the bile ducts, liver disease, or bone disorders.
4. Gamma-glutamyl transferase (GGT): An enzyme found mainly in the liver, pancreas, and biliary system. Increased GGT levels can suggest liver disease, alcohol consumption, or the use of certain medications.
5. Bilirubin: A yellowish pigment produced when hemoglobin from red blood cells is broken down. Bilirubin is processed by the liver and excreted through bile. High bilirubin levels can indicate liver dysfunction, bile duct obstruction, or certain types of anemia.
6. Albumin: A protein produced by the liver that helps maintain fluid balance in the body and transports various substances in the blood. Low albumin levels may suggest liver damage, malnutrition, or kidney disease.
7. Total protein: A measure of all proteins present in the blood, including albumin and other types of proteins produced by the liver. Decreased total protein levels can indicate liver dysfunction or other medical conditions.

These tests are often ordered together as part of a routine health checkup or when evaluating symptoms related to liver function or disease. The results should be interpreted in conjunction with clinical findings, medical history, and other diagnostic tests.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

... prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase. De-Eknamkul W, Ellis BE (1988). " ... In enzymology, an aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction L- ... The systematic name of this enzyme class is L-arogenate:oxaloacetate aminotransferase. Other names in common use include ... whereas its two products are prephenate and L-aspartate. This enzyme belongs to the family of transferases, specifically the ...
... aspartate aminotransferase 1)". Panteghini M (1990). "Aspartate aminotransferase isoenzymes". Clin. Biochem. 23 (4): 311-9. doi ... Totan A, Greabu M, Totan C, Spinu T (2006). "Salivary aspartate aminotransferase, alanine aminotransferase and alkaline ... Aspartate aminotransferase, cytoplasmic is an enzyme that in humans is encoded by the GOT1 gene. Glutamic-oxaloacetic ... Doyle JM, Schininà ME, Bossa F, Doonan S (1990). "The amino acid sequence of cytosolic aspartate aminotransferase from human ...
The systematic name of this enzyme class is L-aspartate:phenylpyruvate aminotransferase. This enzyme is also called aspartate- ... phenylpyruvate aminotransferase. Holger Z, Kula MR (1985). "Isolation and characterization of a highly inducible L-aspartate- ... In enzymology, an aspartate-phenylpyruvate transaminase (EC 2.6.1.70) is an enzyme that catalyzes the chemical reaction L- ... the two substrates of this enzyme are L-aspartate and phenylpyruvate, whereas its two products are oxaloacetate and L- ...
... increased levels of an enzyme called aspartate aminotransferase; headache; and infection in the lungs (pneumonia). Trilaciclib ...
... (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic ... Aminotransferase is cleared by sinusoidal cells in the liver. Aspartate transaminase catalyzes the interconversion of aspartate ... Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S (January 1996). "An aspartate aminotransferase from an extremely ... Kondo K, Wakabayashi S, Yagi T, Kagamiyama H (July 1984). "The complete amino acid sequence of aspartate aminotransferase from ...
... inhibits aspartate aminotransferase, another PLP-dependent enzyme, which is an essential part of the malate ... Also, the inhibition of aspartate aminotransferase by aminooxyacetic acid has clinical implications for the treatment of breast ... Moreover, selective inhibition of aspartate aminotransferase with aminooxyacetic acid ameliorated experimental autoimmune ... "Targeting aspartate aminotransferase in breast cancer". Breast Cancer Research. 10 (5): R84. doi:10.1186/bcr2154. PMC 2614520. ...
Mavrides C, Orr W (1975). "Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli". J. Biol. ... Other names in common use include aromatic amino acid aminotransferase, aromatic aminotransferase, and ArAT. This enzyme ... The systematic name of this enzyme class is aromatic-amino-acid:2-oxoglutarate aminotransferase. ...
September 1975). "The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having ...
ISBN 0-412-46620-1. MURAO, Sawao; NISHINO, Toyokazu; MAEDA, Yasuhiro (1984). "Cytosolic aspartate aminotransferase inactivating ...
Fasella, Paolo; Giartosio, Anna; Hammes, Gordon G. (1966). "The Interaction of Aspartate Aminotransferase with α-Methylaspartic ... He studied the kinetic behavior of various enzymes, including glutamate-aspartate transaminase, hexokinase, and ribonuclease. ...
... aspartate is converted by cytosolic aspartate aminotransferase to oxaloacetate. The net effect of the malate-aspartate shuttle ... by mitochondrial aspartate aminotransferase. Since aspartate is an amino acid, an amino radical needs to be added to the ... aspartate aminotransferase in the mitochondrial matrix and intermembrane space. malate-alpha-ketoglutarate antiporter in the ... glutamate-aspartate antiporter in the inner membrane. The primary enzyme in the malate-aspartate shuttle is malate ...
... elevated levels of the liver enzymes alanine aminotransferase (ALT) and aspartate aminotransferase (AST); and abnormalities in ...
Aspartate aminotransferase, mitochondrial is an enzyme that in humans is encoded by the GOT2 gene. Glutamic-oxaloacetic ... Guidetti P, Amori L, Sapko MT, Okuno E, Schwarcz R (Jul 2007). "Mitochondrial aspartate aminotransferase: a third kynurenate- ... Furuya E, Yoshida Y, Tagawa K (May 1979). "Interaction of mitochondrial aspartate aminotransferase with negatively charged ... "Entrez Gene: GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)". Ford GC, Eichele G, ...
It is also a member of the broader aspartate aminotransferase family. Like many other PLP-dependent enzymes, cystathionine γ- ...
The alanine aminotransferase, aspartate aminotransferase and creatine kinase levels may be raised. The gamma- ...
Guidetti P, Amori L, Sapko MT, Okuno E, Schwarcz R (July 2007). "Mitochondrial aspartate aminotransferase: a third kynurenate- ... kynurenine aminotransferase, and L-kynurenine aminotransferase. This enzyme participates in tryptophan metabolism. It employs ... "Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II". Bioscience Reports ... "Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II". Bioscience Reports ...
The two common types of aminotransferases are alanine aminotransferase (ALT) and aspartate aminotransferase (AST). Booth, ... Glutamate + oxaloacetate ↔ α-ketoglutarate + aspartate Transamination catalyzed by aminotransferase occurs in two stages. In ... Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual ... The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced ...
The enzyme increase is due to an increase in aspartate aminotransferase, glutamate dehydrogenase, and γ-glutamyltransferase.) " ...
The ratio of aspartate aminotransferase to alanine aminotransferase is usually 2 or more. In most cases, the liver enzymes do ... Sorbi D, Boynton J, Lindor KD (1999). "The ratio of aspartate aminotransferase to alanine aminotransferase: potential value in ... and aminotransferases, and onset of jaundice within the last 8 weeks. ...
For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate. Other ... Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form ... Aspartate, glycine, and glutamine are precursors of nucleotides. However, not all of the functions of other abundant ... The two negatively charged amino acids at neutral pH are aspartate (Asp, D) and glutamate (Glu, E). The anionic carboxylate ...
"Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70". The Journal ...
"Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure". Journal of Molecular Biology ... These reactions are facilitated by transaminases in order to produce aspartate and asparagine from oxaloacetate. Transamination ...
"Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure". Journal of Molecular Biology ... In ATCase such a transfer is written as carbamoyl phosphate + L-aspartate → {\displaystyle \rightarrow } L-carbamoyl aspartate ... Transamination, or the transfer of an amine (or NH2) group from an amino acid to a keto acid by an aminotransferase (also known ... This includes enzymes like transaminase (also known as "aminotransferase"), and a very small number of oximinotransferases and ...
Aspartate aminotransferase to platelet ratio index may be used when cost is an issue. Hepatitis B virus DNA remains in the body ... Carriers of the virus may have chronic hepatitis B, which would be reflected by elevated serum alanine aminotransferase (ALT) ... Chronically infected individuals with persistently elevated serum alanine aminotransferase, a marker of liver damage, and HBV ...
... is an irreversible inhibitor of the aspartate aminotransferase produced by the bacterium Streptomyces sumanensis. Its ...
"Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic ... "Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent ... In the absence of glutamate, aspartate can act as the amino donor in the reaction without the need for a different enzyme, but ... Glutamate-prephenate aminotransferase catalyzes the reversible reaction shown below: , and its primary purpose is to convert ...
Here, the OAA produced by PEPC is transaminated by aspartate aminotransferase to aspartate (ASP) which is the metabolite ... In this variant the OAA produced by aspartate aminotransferase in the bundle sheath is decarboxylated to PEP by PEPCK. The fate ... The first experiments indicating that some plants do not use C3 carbon fixation but instead produce malate and aspartate in the ... either malate or aspartate) in the mesophyll. The organic acids then diffuse through plasmodesmata into the bundle sheath cells ...
"Severe preeclampsia with fulminant and extreme elevation of aspartate aminotransferase and lactate dehydrogenase levels: high ... an aspartate transaminase greater than 70 U/L, and platelets less than 100×109/l. If not all the criteria are present, the ... and aspartate transaminase (AST), are indicative of hepatic dysfunction. Extremely high serum levels of these proteins, ...
Hsu YC, Tai DI (2011). "Unusually high alanine aminotransferase to aspartate aminotransferase ratio in a patient with ...
... may cause severe elevations in serum aminotransferases, alanine transaminase (ALT) and aspartate ...
... prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase. De-Eknamkul W, Ellis BE (1988). " ... In enzymology, an aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction L- ... The systematic name of this enzyme class is L-arogenate:oxaloacetate aminotransferase. Other names in common use include ... whereas its two products are prephenate and L-aspartate. This enzyme belongs to the family of transferases, specifically the ...
The aspartate aminotransferase (AST) blood test measures the level of the enzyme AST in the blood. ... The aspartate aminotransferase (AST) blood test measures the level of the enzyme AST in the blood. ...
The blood test for aspartate transaminase (AST) is usually carried out to detect liver damage. The test is always done in ... Test : Aspartate transaminase. Indications : An AST test is ordered for the following reasons -. When a person shows symptoms ... Physiology : The blood test for aspartate transaminase (AST) is usually carried out to detect liver damage. The test is always ... done in combination with the test for another liver enzyme, alanine amino transferase (ALT), to help diagnose liver problems. ...
Performance of the aspartate aminotransferase-to-platelet ratio index for the staging of hepatitis C-related fibrosis: an ... The aspartate aminotransferase-to-platelet ratio index (APRI), a tool with limited expense and widespread availability, is a ...
... Journal ... Preliminary study of aspartate aminotransferase activity in GCF during orthodontic tooth movement. J. Applied Oral Sci.. ... The Activity of Aspartate Aminotransferase During Canine Retraction (Bodily Tooth Movement) in Orthodontic Treatment table, th ... Aspartate aminotransferase activity in pulp of orthodontically treated teeth. Am. J. Orthod. Dentofacial. Orthop., 125: 88-92. ...
aspartate aminotransferase answers are found in the Tabers Medical Dictionary powered by Unbound Medicine. Available for ... "Aspartate Aminotransferase." Tabers Medical Dictionary, 24th ed., F.A. Davis Company, 2021. Nursing Central, nursing. ... unboundmedicine.com/nursingcentral/view/Tabers-Dictionary/744563/0/aspartate_aminotransferase. Aspartate aminotransferase. In: ... Aspartate Aminotransferase [Internet]. In: Venes DD, editors. Tabers Medical Dictionary. F.A. Davis Company; 2021. [cited 2023 ...
Betapace and Aspartate Aminotransferase Increased. This page shows results related to Betapace and Aspartate Aminotransferase ...
An AST blood test measures the level of AST in your blood sample.
LBXSASSI - Aspartate aminotransferase AST (U/L). Variable Name: LBXSASSI. SAS Label: Aspartate aminotransferase AST (U/L). ... Aspartate aminotransferase AST (U/L). Target: Both males and females 12 YEARS - 150 YEARS. Code or Value. Value Description. ... 3. Aspartate Aminotransferase (AST) The DxC800 uses an enzymatic rate method to measure the AST activity in serum or plasma. In ... 4. Aspartate Aminotransferase (AST) AST measurements are used in the diagnosis and treatment of certain types of liver and ...
Aspartate Aminotransferase (AST) Polyclonal Antibody, Cat#CAU26353. Rating Required Select Rating. 1 star (worst). 2 stars. 3 ... cCAT; AAT; ASAT; SGOT; GOT1; Cysteine transaminase, cytoplasmic; Transaminase A; Aspartate Transaminase 1,Cytoplasmic; Glutamic ...
Human AST(Aspartate Aminotransferase) ELISA Kit. Human AST(Aspartate Aminotransferase) ELISA Kit. To Order: [email protected] ... Description: A sandwich ELISA kit for detection of Aspartate Aminotransferase from Human in samples from blood, serum, plasma, ... Description: A sandwich ELISA kit for detection of Aspartate Aminotransferase from Human in samples from blood, serum, plasma, ... Description: A sandwich quantitative ELISA assay kit for detection of Human Aspartate Aminotransferase (AST) in samples from ...
The reference range for aspartate aminotransferase (AST) is as follows: Males: 6-34 IU/L Females: 8-40 IU/L ... encoded search term (Aspartate Aminotransferase) and Aspartate Aminotransferase What to Read Next on Medscape ... Aspartate Aminotransferase Updated: Jan 13, 2015 * Author: Sridevi Devaraj, PhD, DABCC, FACB; Chief Editor: Thomas M Wheeler, ... Conditions associated with very high aspartate aminotransferase levels (more than 10 times the highest normal value) are as ...
The reference range for aspartate aminotransferase (AST) is as follows: Males: 6-34 IU/L Females: 8-40 IU/L ... encoded search term (Aspartate Aminotransferase) and Aspartate Aminotransferase What to Read Next on Medscape ... Aspartate Aminotransferase Updated: Jan 13, 2015 * Author: Sridevi Devaraj, PhD, DABCC, FACB; Chief Editor: Thomas M Wheeler, ... Conditions associated with very high aspartate aminotransferase levels (more than 10 times the highest normal value) are as ...
Aspartate Aminotransferase) plays a critical role in amino acid and carbohydrate metabolism. The AST blood test is used to ... What is the role of AST Aspartate Aminotransferase?. The AST (Aspartate Aminotransferase), formerly named glutamate ... Thomas L. Alanine aminotransferase (ALT), Aspartate aminotransferase (AST). In:Thomas L, ed. Clinical laboratory diagnostics. ... The AST (Aspartate Aminotransferase) blood test is used to diagnose liver disorders. It may also indicate cardiac disease. ...
Aspartate Aminotransferase (AST/SGOT) (LabCorp). Get know how much does lab test cost. Direct access testing with or without ... Aspartate Aminotransferase (AST/SGOT) Aspartate Aminotransferase (AST/SGOT) Lab Test Short Info. Screening for the next ... Aspartate Aminotransferase (AST/SGOT) in online lab tests stores. If you need more than just Aspartate Aminotransferase (AST/ ... Aspartate Aminotransferase (AST/SGOT) test cost is between $29.99 and $58.00. None Aspartate Aminotransferase (AST/SGOT) test ...
... The aspartate aminotransferase (AST) take a look ... It is usually ordered with a take a look at for alanine aminotransferase (ALT), one other liver enzyme. ...
Elevated alanine aminotransferase or aspartate aminotransferase levels of unknown origin. *Persons who request HBV testing (new ... aspartate aminotransferase/alanine aminotransferase; CBC = complete blood count; HBeAg = hepatitis B e antigen; HBsAg = ... Persons with Elevated ALT or Aspartate Aminotransferase Levels of Unknown Origin. Persons with known chronic liver disease (e.g ... However, persons with persistently elevated ALT or aspartate aminotransferase (AST) levels without a known cause should be ...
ALANINE AMINOTRANSFERASE/ASPARTATE AMINOTRANSFERASE RATIO REVERSAL AND PROLONGED PROTHROMBIN TIME: A SPECIFIC INDICATOR OF ...
Coli Aspartate Aminotransferase. To be Published Release Date. 1994-04-30. Peptides. ASPARTATE AMINOTRANSFERASE: AB. SMTL:PDB. ... THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE ...
... alanine aminotransferase, aspartate aminotransferase, serum creatinine, C-reactive protein, total bilirubin, total cholesterol ...
Slide 7: Aspartate Aminotransferase (AST). AST is not specific to the liver and is also found in the kidney and cardiac and ... Her lab tests are remarkable for an elevated aspartate amino transferase or AST ~10 times the upper limit of the reference ... Slide 12: Alanine Aminotransferase (ALT). Alanine amino transferase or ALT is also a transaminase and is considered to be the ... The aminotransferase enzymes, ALT and AST, are indicators of liver cell death and can be used to answer the questions: What is ...
Aspartate aminotransferase. AUC:. Area under the curve. BCLC:. Barcelona Clinic Liver Cancer ...
Aspartate Aminotransferase (AST). AST is an enzyme found throughout the body. Elevated concentration levels of AST in the blood ... Alanine Aminotransferase (ALT). ALT is one of the enzymes within the aminotransferases group and are among the most sensitive ... Aminotransferases are a family of enzymes that catalyse the conversion of amino acids to 2-oxo-acids by the transfer of amino ... Elevations of aminotransferase is the most common abnormality in patients presenting with COVID-19. It was identified that AST ...
However, the highest performances after N90 were accompanied with lesser aspartate aminotransferase (P , .001, d = 1.74) and ... PSD increased postexercise aspartate aminotransferase (P , .001, d = 4.16) and decreased glutathione peroxidase (P , .001, d = ...
Abbreviations: ALT = alanine aminotransferase; AST = aspartate aminotransferase; ED = emergency department; HR = heart rate; O2 ...
Aspartate aminotransferase. You may have a blood test for ALP to detect liver disease.. ... Alanine aminotransferase. You may have a blood test for ALP to detect liver disease.. ...
Aspartate aminotransferases, IU/L‡ Nov 2008. 53. ND. Dec 2008. 30. 21. ...
Aspartate Aminotransferase (AST). [PDF - 235 KB] September 2011. Bicarbonate (HCO3). [PDF - 416 KB] September 2011. ...
... aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), total protein (TP), albumin (Alb ... W. R. Kim, S. L. Flamm, A. M. Di Bisceglie, and H. C. Bodenheimer, "Serum activity of alanine aminotransferase (ALT) as an ...
Your Search: (SUBJECT=Aminotransferases aspartate) Sort Results: Publication dates (newest-oldest). Publication dates (oldest- ...
  • Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase. (wikipedia.org)
  • The blood test for aspartate transaminase (AST) is usually carried out to detect liver damage . (medindia.net)
  • Aspartate transaminase catalyzes the interconversion of aspartate and α-ketoglutarate to glutamate. (medscape.com)
  • The AST (Aspartate Aminotransferase), formerly named glutamate oxaloacetate transaminase (GOT), is an enzyme of the transaminase group. (mrlabtest.com)
  • Aspartate aminotransferase (glutamate oxalacetate transaminase) belongs to the transaminases, which catalyze the interconversion of amino acids and α‑ketoacids by transfer of amino groups. (unitslab.com)
  • At the outside hospital, she was noted to have mild transaminitis (alanine transaminase [ALT] 205 U/L, aspartate transaminase [AST] 357 U/L) and persistent fevers. (thieme-connect.de)
  • If you need more than just Aspartate Aminotransferase (AST/SGOT) lab test - add more tests one by one. (findlabtest.com)
  • None Aspartate Aminotransferase (AST/SGOT) test cost minimal is in RequestATest (Aspartate Aminotransferase (AST) Blood Test) with price $34.00. (findlabtest.com)
  • Aspartate Aminotransferase (AST/SGOT) test cost max is in Personalabs (AST SGOT Blood Test) with price $51.00. (findlabtest.com)
  • Serum elevations of ALT activity are rarely observed except in parenchymal liver disease, since ALT is a more liver-specific enzyme than aspartate aminotransferase (AST). (cdc.gov)
  • Description: Quantitativesandwich ELISA kit for measuring Human Aspartate aminotransferase, AST in samples from serum, plasma, tissue homogenates. (elisastrip.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Aspartate Aminotransferase (AST) in samples from serum, plasma, tissue homogenates or other biological fluids. (elisastrip.com)
  • Description: A sandwich ELISA for quantitative measurement of Human Aspartate aminotransferase,AST in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (elisastrip.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Aspartate Aminotransferase (AST) in serum, plasma, tissue homogenates, cell lysates and other biological fluids. (elisastrip.com)
  • Wai's aspartate-aminotransferase (AST) to platelet ratio index (APRI) was calculated from serum AST and blood platelet number. (akjournals.com)
  • and alanine aminotransferase {ALT} 138 U/L {normal: 7-56 U/L}). Although he reported no abdominal pain and the abdominal examination on admission was normal, serum amylase and lipase levels were elevated (amylase 226 U/L {normal: 30-110 U/L} and lipase 771 U/L {normal: 23-300 U/L}). Chest radiographs at the time of admission demonstrated perihilar interstitial infiltrates. (cdc.gov)
  • Acute viral hepatitis, drug or toxin induced liver disease and ischaemic liver injury are characterised by extremely elevated aminotransferase levels 3 . (randox.com)
  • Participants were classified as having elevated aminotransferase levels if either aspartate aminotransferase or alanine aminotransferase was elevated above normal. (nih.gov)
  • In enzymology, an aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction L-arogenate + oxaloacetate ⇌ {\displaystyle \rightleftharpoons } prephenate + L-aspartate Thus, the two substrates of this enzyme are L-arogenate and oxaloacetate, whereas its two products are prephenate and L-aspartate. (wikipedia.org)
  • The systematic name of this enzyme class is L-arogenate:oxaloacetate aminotransferase. (wikipedia.org)
  • The aspartate aminotransferase (AST) blood test measures the level of the enzyme AST in the blood. (medlineplus.gov)
  • The pattern of activity of aspartate aminotransferase enzyme (AST) following canine distalization stage in orthodontic treatment is being investigated. (scialert.net)
  • The current study which investigated the pattern of aspartate aminotransferase (AST) activity following application of force to distalize the canine (100 g) was a continuation of an earlier study by the same researcher which investigated the enzyme`s activity after the application of force to align teeth (30-60 g). (scialert.net)
  • Another enzyme, alanine aminotransferase or ALT, is primarily found in the liver. (medscape.com)
  • It is usually ordered with a take a look at for alanine aminotransferase (ALT), one other liver enzyme. (fairpeel.com)
  • We have cloned and characterized a mouse cytosolic aspartate aminotransferase (AspAT) (EC 2.6.1.1) gene, which is about 32,000 base-pairs long and is interrupted by eight introns. (elsevierpure.com)
  • The aspartate aminotransferase-to-platelet ratio index (APRI), a tool with limited expense and widespread availability, is a promising noninvasive alternative to liver biopsy for detecting hepatic fibrosis. (nih.gov)
  • Objectives: The objectives of the current study were to associate novel markers, including aspartate aminotransferase-to-platelet ratio (APRI) and aspartate aminotransferase-to-alanine aminotransferase ratio (AAR) with survival in esophageal malignancy. (aku.edu)
  • This study aimed to evaluate the diagnostic performances of aspartate aminotransferase to platelet ratio index (APRI) and fibrosis 4 (FIB‐4) scores compared with TE. (thasl.org)
  • Alanine aminotransferase measurements are used in the diagnosis and treatment of certain liver diseases (e.g., viral hepatitis and cirrhosis) and heart diseases. (cdc.gov)
  • Aminotransferase elevation was classified as "explained" if there was laboratory evidence of hepatitis B or C infection, iron overload, or if there was a history of alcohol consumption. (nih.gov)
  • Aminotransferase elevation was common in the United States, and the majority could not be unexplained by alcohol consumption, viral hepatitis or hemochromatosis. (nih.gov)
  • Out of 119 HCV-infected patients, 75 had biopsy-proven chronic hepatitis C, 24 had HCV cirrhosis, 20 individuals were symptom-free HCV carriers with persistently normal alanine aminotransferase (PNA), and 30 healthy blood donors served as controls. (akjournals.com)
  • Structural organization of the mouse aspartate aminotransferase isoenzyme genes. (elsevierpure.com)
  • Dive into the research topics of 'Structural organization of the mouse aspartate aminotransferase isoenzyme genes. (elsevierpure.com)
  • Unexplained aminotransferase elevation was strongly associated with adiposity and other features of the metabolic syndrome, and thus may represent nonalcoholic fatty liver disease. (nih.gov)
  • The aminotransferase enzymes, ALT and AST, are indicators of liver cell death and can be used to answer the questions: What is the extent of hepatic damage or how many liver cells died in the last 24 hours? (aacc.org)
  • Aminotransferases are a family of enzymes that catalyse the conversion of amino acids to 2-oxo-acids by the transfer of amino acids 1 . (randox.com)
  • Immediately discontinue maraviroc and other suspected agents if signs or symptoms of severe skin or hypersensitivity reactions develop and monitor clinical status, including liver aminotransferases, closely. (drugs.com)
  • Each laboratory must establish its own normal ranges for AST (aspartate aminotransferase) in the blood. (mrlabtest.com)
  • Baseline viral load and alanine aminotransferase level in addition to early virological response to pegylated interferon-based therapy may serve as a decision tool for clinicians to identify patients who are unlikely to achieve SVR. (who.int)
  • The AST (Aspartate Aminotransferase) blood test is used to diagnose liver disorders. (mrlabtest.com)
  • The AST concentration in the blood is closely related to the ALT (alanine aminotransferase) concentration. (mrlabtest.com)
  • The aspartate aminotransferase (AST) take a look at is a blood take a look at that checks for liver injury. (fairpeel.com)
  • The aminotransferases are very important for detecting acute liver disease. (aacc.org)
  • Although often used to detect liver disease, the prevalence and etiology of elevated aminotransferases are unknown. (nih.gov)
  • This page shows results related to Betapace and Aspartate Aminotransferase Increased from the FDA Adverse Event Reporting System (AERS). (drugcite.com)
  • Her lab tests are remarkable for an elevated aspartate amino transferase or AST ~10 times the upper limit of the reference range. (aacc.org)
  • Aspartate aminotransferase is commonly found in human tissue. (unitslab.com)
  • Elevations of aminotransferase is the most common abnormality in patients presenting with COVID-19. (randox.com)
  • Share your experience with Betapace and Aspartate Aminotransferase Increased. (drugcite.com)
  • Aspartate aminotransferase also reportedly reflects gonadal function and the amount of oxygen available to membranes. (drkaslow.com)
  • For example, elevated alanine transaminase and aspartate transaminase disproportional to bilirubin and alkaline phosphatase levels often indicates liver disease. (healthline.com)
  • Serum triglyceride (TG), total-cholesterol (T-cho), glucose (Glu), alanine transaminase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), geranylgeranyltransferase (GGT) and albumin (Alb) levels were measured. (spandidos-publications.com)
  • TMF-treated rats showed significantly lower relative enhancement (RE) values and serum alanine aminotransferase (ALT) and aspartate aminotransferase levels than did untreated rats at three hours after reperfusion. (researchsquare.com)
  • To assess the diagnostic value of modified cutoffs for aspartate aminotransferase to platelet ratio index (APRI) to predict significant liver fibrosis in human immunodeficiency virus (HIV)/hepatitis C virus (HCV) patients. (medscape.com)
  • Objective To analyze the relationship between aspartate aminotransferase to platelet ratio index (APRi) and liver injury occurrence in pediatric sepsis, as well as determine the APRi cutoff value for early identification of SALI. (paediatricaindonesiana.org)
  • 6. Unlusoy-Aksu A, Sari S, Yilmaz G, Egritas-Gurkan O, Demitras Z, Dalgic B. Aspartate aminotransferase-to-platelet ratio index in children with cholestatic liver diseases to assess liver fibrosis. (paediatricaindonesiana.org)
  • 7. Grieve A, Makin E, Davenport M. Aspartate aminotransferase-to-platelet ratio index (APRi) in infants with biliary atresia: prognostic value at presentation. (paediatricaindonesiana.org)
  • 8. Hwang JH, Chung ML. Predictive value of the aspartate aminotransferase to platelet ratio index for parenteral nutrition associated cholestasis in extremely low birth weight infants. (paediatricaindonesiana.org)
  • Mapping of the aspartate and aromatic amino acid amino-transferase genes tyrB and aspC. (yale.edu)
  • The most common laboratory abnormalities (≥15%) were increased glucose, triglycerides, alanine aminotransferase, and aspartate aminotransferase. (fda.gov)
  • Aspartate transaminase catalyzes the interconversion of aspartate and α-ketoglutarate to glutamate. (medscape.com)
  • Aspartate aminotransferase (AAT) is a prototypical pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes the reversible interconversion of l-aspartate and α-ketoglutarate with oxalacetate and l-glutamate via a ping-pong catalytic cycle in which the pyridoxamine 5'-phosphate enzyme form is an intermediate. (nih.gov)
  • A Dynamic Aspartate-to-Alanine Aminotransferase Ratio Provides Valid Predictions of Incident Severe Liver Disease. (sdu.dk)
  • The aspartate‐to‐alanine aminotransferase ratio (AAR) is associated with liver fibrosis, but its predictive performance is suboptimal. (sdu.dk)
  • In enzymology, an aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction L-arogenate + oxaloacetate ⇌ {\displaystyle \rightleftharpoons } prephenate + L-aspartate Thus, the two substrates of this enzyme are L-arogenate and oxaloacetate, whereas its two products are prephenate and L-aspartate. (wikipedia.org)
  • Risk prediction following acetaminophen (paracetamol, APAP) overdose is based on serum APAP, aspartate aminotransferase (AST), and alanine aminotransferase (ALT) levels. (nih.gov)
  • Having this background, the present study was designed to investigate the correlation between the levels of serum liver enzymes alanine aminotransferase (ALT), aspartate aminotransferase (AST) and GGT and Asia-Pacific cut-off points of BMI in healthy individuals. (springeropen.com)
  • Main outcome measures Scores on alcohol use disorders identification test and measures of γ-glutamyltransferase, aspartate aminotransferase, per cent carbohydrate deficient transferrin, and erythrocyte mean cell volume. (bmj.com)
  • Results A significant correlation was observed be alcohol consumption and score on the alcohol use disorders identification test (Pearson's correlation coefficient r = 0.74) and measures of γ-glutamyltransferase (r = 0.20) and per cent carbohydrate deficient transferrin (r = 0.36) but not aspartate aminotransferase (r = 0.08) or erythrocyte mean cell volume (r = 0.02). (bmj.com)
  • The aspartate aminotransferase (AST) blood test measures the level of the enzyme AST in the blood. (medlineplus.gov)
  • The aspartate aminotransferase (AST) test is a blood test that checks for liver damage. (maxtechhealth.com)
  • Liver function test also revealed increased aspartate aminotransferase (AST) (164 U/L, normal range: 0-40 U/L), gamma-glutamyl transpeptidase (GGT) 243 U/L (normal range: 0-43 U/L), and decreased cholinesterase (2294 U/L, normal range: 5000-12,000 U/L). The IgM of toxoplasma, rubella virus, herpes simplex virus, and cytomegalovirus (CMV) were negative. (springer.com)
  • Plasma alanine aminotransferase (ALT), measured at 24-hour intervals from 24-96 hours after dosing and evaluated as the area under the curve (AUC), was significantly lower in the mixture groups than predicted by the sum of measured responses to each chemical alone, indicating a less-than-effect-additive joint toxic action. (cdc.gov)
  • Serum elevations of ALT activity are rarely observed except in parenchymal liver disease, since ALT is a more liver-specific enzyme than aspartate aminotransferase (AST). (cdc.gov)
  • Kolb VG, Kamyshnikov VS (1976)Colorimetric dinitrophenylhydrazine method for determining the activity of aminotransferases in blood serum. (scholarena.co)
  • Osadchaya LM (1982).Determination of aminotransferase activity in tissues. (scholarena.co)
  • Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase. (wikipedia.org)
  • AST ( Aspartate Aminotransferase) used to detect damage to cells. (quickdrawlab.com)