Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The biochemical characterization of experimental acute pancreatitis was performed by determination of the secretory enzymes lipase and alpha-amylase, of the cytoplasmic ALAT (alanine aminotransferase), of total protein and calcium concentration in serum of rats. The moderate and protracted course of the pathological process in the small animal model presented allowed to study the initial phase from 1-24 h. In the first 4-8 h most massive enzyme release into the intravasal space was observed. The level of enzyme activities was correlating with the severity of assault. One noxa alone (ischemia or juice edema) resulted in a moderate enzyme release (lipase : 2-2.5 fold of control). The action of both noxae caused a drastical increase in enzyme activities in the initial phase lipase : 8-20 fold, ALAT: 7 fold, alpha-Amylase: 2.5 fold). 24 h postoperatively the serum enzyme activities were at distinct pathological level. At this time acute pancreatitis provoked already a decreased serum protein content. A hypocalcemia was not observed.
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PMID:Contribution of pancreatic edema and short-term ischemia to experimental acute pancreatitis in the rat. II. Behaviour of serum parameters. 349 93

Using fully mechanized analytical equipment, interference by haemolysis in the determination of 26 clinical chemical parameters was determined quantitatively by adding haemolysate to serum. Haemoglobin concentrations up to 6.6 g/l caused essentially no interference in the following determinations: albumin (immuno-nephelometric), alpha-amylase, calcium, chloride, cholesterol, cholinesterase, creatinine, iron, glucose, glutamate dehydrogenase, uric acid, urea, sodium, inorganic phosphate, total protein, transferrin and triglycerides. In the presence of haemoglobin, erroneously high values were found for: lactate dehydrogenase (haemoglobin higher than 0.2 g/l), aspartate aminotransferase, potassium and acid phosphate (haemoglobin higher than 1.5 g/l), creatine kinase (haemoglobin higher than 2.5 g/l) and alanine aminotransferase (haemoglobin higher than 3.4 g/l). Erroneously low values were found for bilirubin (haemoglobin higher than 0.8 g/l), alkaline phosphatase and albumin (by electrophoresis) (haemoglobin higher than 1.5 g/l) and gamma-glutamyltransferase (haemoglobin higher than 3.0 g/l).
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PMID:Haemolysis as an interference factor in clinical chemistry. 371 97

The effect of dichlorvos and metathion was studied as exerted on acetylcholinesterase activity in the protozoan Tetrahymena pyriformis. In dichlorvos, the highest enzyme activity inhibition was obtained after 30 minutes. A 50% inhibition of the enzyme activity was recorded at the dose of 1.22 mg per litre. As to metathion, the highest enzyme activity inhibition was obtained after 60 minutes. A 50% inhibition of the enzyme activity was recorded at the dose of 879.2 ng per litre. One hour after exposure to this dose, almost 75% inhibition of the activity of the enzyme was recorded. The determination of acetylcholinesterase activity increases the sensitivity of the bioassay for organophosphates with the use of the Tetrahymena pyriformis protozoan. Dichlorvos was studied for its action at supratoxic doses (50.0, 100.0 and 150.0 mg per litre) and it was found that lactate dehydrogenase activity was almost completely suppressed; the inhibition of alanine aminotransferase was pronounced. A weaker activity inhibition was recorded in aspartate aminotransferase, alkaline and acid phosphatase; the activity of alpha-amylase increased. No dependence on dosage was demonstrated.
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PMID:[The effect of dichlorvos and metathion on selected enzymes of the amoeba Tetrahymena pyriformis]. 392 68

We analyzed the stability of the enzymes alpha-amylase (EC 3.2.1.1), alkaline phosphatase (EC 3.1.3.1), alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1), creatine kinase (EC 2.7.3.2), glutamate dehydrogenase (EC 1.4.1.3), gamma-glutamyltransferase (EC 2.3.2.2) and lactate dehydrogenase (EC 1.1.1.27) of a human serum pool during storage in liquid nitrogen for a period of 10 months. Except amylase and creatine kinase, all enzymes were stable. Amylase increased in activity, creatine kinase activity decreased. Therefore, human serum stored at -196 degrees C can be used as satisfactory substitute for lyophilized enzyme control serum in internal quality control and stable enzyme material for optimization of methods.
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PMID:Long-term stability of enzymes in human serum stored in liquid nitrogen. 614 44

Activities of alpha-hydroxybutyrate- and lactate dehydrogenases (HBDH, LDH), aspartate- and alanine aminotransferases (AST, ALT), alkaline phosphatase, alpha-amylase as well as content of total proteins, glucose, cholesterol, triglycerides and Ca2+ were estimated sprectrophotometrically in blood serum of rat males within 2 hrs after thermic burns of the III degree involving 15% the body surface. The burns caused about 2-fold increase in activities of LDH, HBDH and AST and in content of triglycerides in blood serum but did not affect the other biochemical patterns. Adrenalectomy, carried out within 3 days before the burns, accelerated and pseudoadrenalectomy decreased the early postburn enzymatic activation. Preadministration of reserpine, phentolamine and obsidane (propranolol) decreased distinctly the hyperenzymic reaction observed after the burn stress.
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PMID:[Effect of adrenalectomy and anti-adrenergic preparations on the development of hyperenzymic and biochemical changes in the blood in burns]. 620 53

Aiming at an improvement of the screening of toxic substances in biological materials and environment, the following biochemical indices were studied by means of the Tetrahymena pyriformis as a testing object: total protein, total lipids, glucose, lactate dehydrogenase (E.C.1.1.1.27.), gamma-glutamyl transferase (E.C.2.3.2.2.), aspartate aminotransferase (E.C.2.6.1.1.), alanine aminotransferase (E.C.2.6.1.2.), acetyl cholinesterase (E.C.3.1.1.7.), butyryl cholinesterase (E.C.3.1.1.8.), alkaline phosphatase (E.C.3.1.3.1.), acid phosphatase (E.C.3.1.3.2.) and alpha-amylase (E.C.3.2.1.1.). The study was conducted in the period of the population growth in an experimental medium with the minimum content of nutrients within the 96 hours of cultivation. It has been derived from the results that most of the enzymes are at the top of their activity in the early logarithmic stage of growth, i. e. in the period immediately following the log stage of population growth when the cells are getting ready for intensive division and growth; another peak activity period is the logarithmic growth stage--alkaline phosphatase and acid phosphatase are an exception with the culmination of activity in the stationary stage of population growth.
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PMID:[Selected biochemical indicators in the protozoan Tetrahymena pyriformis]. 644 37

Activities of 14 enzymes were determined in psoas muscle, smooth muscle, diaphragm, heart, brain, liver, kidney, spleen, pancreas, salivary glands, zygomatic gland, intestinal mucosa, subcellular fractions, and plasma of the dog. In pups, plasma activity of most enzymes was high, except iditol dehydrogenase (ID), glutamate dehydrogenase (GLD), alanine aminotransferase (ALT), aspartate aminotransferase (AST), and D-fructose-1,6-diphosphate aldolase (ALS). Alkaline phosphatase (ALP), ALS, cholinesterase (CHS), creatine kinase (CK), alpha-hydroxybutyrate dehydrogenase (HBD), lactate dehydrogenase (LD), and malate dehydrogenase (MD) decreased significantly (P less than 0.01) with increasing age, but in dogs greater than 7 months, all enzymes except CK, HBD, and ALT revealed reasonably constant plasma values. Enzymes ALT, GLD, CHS, and ID are specific for liver, CK and ALS for muscle, HBD to some degree for myocardium, and alpha-amylase for pancreas. The ALP and gamma-glutamyltransferase were located in microsomes, GLD in mitochondria, MD and AST in mitochondria and cytoplasm, and isocitric dehydrogenase, LD, and the other enzymes only in cytoplasm.
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PMID:Enzyme activities in the dog: tissue analyses, plasma values, and intracellular distribution. 703 2

A multi-enzyme reference material was prepared from seven enzymes of asparatate aminotransferase (AST, EC 2.6.1.1), alanine aminotransferase (ALT, EC 2.6.1.2), alkaline phosphatase (ALP, EC 3.1.3.1), lactate dehydrogenase (LD, EC 1.1.1.27), creatine kinase (CK, EC 2.7.2.2), gamma-glutamyltranspeptidase (gamma-GT, EC 2.3.2.2) and amylase (AMY, EC 3.2.1.1) which were purified from human sources including established human cell lines. The enzymatic properties of the material closely resembled those of human serum. In lyophilized form the preparation was stable for at least 200 days when stored at 40 degrees C. Intermethod comparisons of the enzyme activities in 80 clinical specimens were done by correcting the mean values with calibration constants for different assay methods resulting from use of a human serum, the multi-enzyme reference and a commercial control serum. The results from the comparison for the six enzymes of AST, ALT, LD, CK, gamma-GT and AMY in use of the multi-enzyme reference were almost the same as those with use of a human serum as a calibrator, but were not satisfactory for ALP. Even though further search for more reliable material for ALP is required the multi-enzyme reference material can be used for standardization in clinical chemistry.
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PMID:Multi-enzyme reference material from established human cell lines and human sources. 753 22

We have developed a new multienzyme control serum, Seraclear-HE, which was designed to function not only as an accuracy and precision control serum but also as an intermethod calibrator for unifying interlaboratory clinical enzyme data in terms of reference method values. Seraclear-HE contains as analytes the following enzymes of human origin only: aspartate aminotransferase (AST, EC 2.6.1.1) and lactate dehydrogenase (LD, EC 1.1.1.27) from erythrocytes; alanine aminotransferase (ALT, EC 2.6.1.2) from a hepatoma cell line; alkaline phosphatase (ALP, EC 3.1.3.1) from an amnion cell line; creatine kinase (CK, EC 2.7.3.2) from an embryo kidney cell line; gamma-glutamyltransferase (GGT, EC 2.3.2.2) from a macrophage cell line; and amylase (AMY, EC 3.2.1.1) from urine and saliva. The seven partly purified enzymes were lyophilized in partially delipidated human serum containing sucrose (50 g/L), pyridoxal 5'-phosphate (30 mmol/L), and other stabilizers. The material is stable for at least 2 years at temperatures < or = 10 degrees C. For two concentrations of this preparation, reference method values (mainly International Federation of Clinical Chemistry and Japan Society of Clinical Chemistry) obtained at both 30 degrees C and 37 degrees C are assigned.
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PMID:Multienzyme control serum (Seraclear-HE) containing human enzymes from established cell lines and other sources. 1: Preparation and properties. 753 43

Information on the stability of serum analytes during storage of serum or whole blood samples is often incomplete and sometimes contradictory. Using a widely available analyser (Hitachi 737/Boehringer), we therefore determined the effects of storage time and temperature on the measured concentrations of the following serum analytes: sodium, potassium, calcium, chloride, inorganic phosphate, magnesium, creatinine, urea, uric acid, bilirubin, cholesterol, HDL- and LDL-cholesterol, triacylglycerols, creatine kinase, aspartate aminotransferase, alanine aminotransferase, gamma-glutamyltransferase, alkaline phosphatase, alpha-amylase, lactate dehydrogenase and cholinesterase. When separated serum was stored at + 9 degrees C for seven days, the mean changes in inorganic phosphate and lactate dehydrogenase exceeded significantly (p < 0.05 or 0.001, respectively) the maximum allowable inaccuracy according to the Guidelines of the German Federal Medical Council; all other quantities were sufficiently stable. In serum at room temperature, inorganic phosphate, uric acid, HDL-cholesterol and triacylglycerols increased continuously, whereas bilirubin, LDL-cholesterol, creatine kinase and aspartate aminotransferase decreased more than the guidelines permit during the storage period (p < 0.05 for aspartate aminotransferase, p < 0.001 for the other analytes mentioned). In whole blood stored for 7 days at + 9 degrees C, only the following serum analytes satisfied the stability requirements of the guidelines: calcium, urea, cholesterol, HDL-cholesterol, LDL-cholesterol, triacylglycerols, creatine kinase, gamma-glutamyltransferase and cholinesterase. When stored at room temperature, only sodium, uric acid, bilirubin, cholesterol, triacylglycerols, aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, alpha-amylase and cholinesterase were still stable after 3 days. The data collected show that all quantities examined are sufficiently stable for four days in separated serum stored at + 9 degrees C.
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PMID:Storage of serum or whole blood samples? Effects of time and temperature on 22 serum analytes. 762 90


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