Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Low turbidity, "clear" enzyme controls commercially produced in three concentrations and conventional human lyophilized control sera, which are more turbid, were evaluated to determine which was superior for quality control purposes. Criteria used to evaluate the controls were: 1) turbidity measurement, 2) daily assays for 30 days to estimate day-to-day precision, and 3) stability of the enzyme assay value for these controls when they were reconstituted and frozen for 0 to 30 days and 0 to 10 days with three aliquots separately prepared and frozen for 0 to 10 days for a total of 30 days. The controls were analyzed for lactate dehydrogenase, alanine aminotransferase, aspartate aminotransferase, creatine kinase, and alkaline phosphatase activities with the Perkin-Elmer KA 150 enzyme analyzer.
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PMID:The use of "clear" enzyme control materials. 42 91

Normal values for 13 chemical constituents of plasma were estimated from results for 837 presumably healthy children. Ninety microliters of specimen was analyzed for lactate dehydrogenase, aspartate aminotransferase, alkaline phosphatase, inorganic phosphorus, total calcium, total cholesterol, total proteins, albumin, uric acid, urea nitrogen, alanine aminotransferase, total bilirubin, and glucose. We used two Abbott ABA-100 Bichromatic Analyzers interfaced directly to the ABA Data Management System. For each test age- and sex-related variations were assessed and normal values were estimated for six different age groups.
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PMID:Microchemical analysis for 13 constituents of plasma from healthy children. 43 35

In order to verify the influence of sampling time on blood constituents, populations of supposedly healthy subjects were grouped according to age, sex, deviation from their ideal weight, state of fasting or nonfasting, and time of sampling. Each fasting subject in one group underwent two samplings during the course of a morning: the first at 08.00 and the second between 09.00 and 12.00. In the second group, the first was taken at 13.00, and the second between 14.00 and 16.00. Subjects in the second group had eaten a standard meal of 700 calories at 12.00. Differences between the paired samples from a given individual are discussed with respect to the time of sampling for plasma urea, creatinine, proteins, albumin, calcium, sodium, potassium, cholesterol, uric acid, chloride ions, phosphate, bilirubin, aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase, creatine phosphokinase, alkaline phosphatase, hemoglobin and erythrocyte and leukocyte counts. Variations due to the time of sampling were large for phosphorus, bilirubin, and leukocyte count.
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PMID:The effect of sex, deviation from ideal weight and sampling time on blood constituents in presumably healthy subjects. 43 75

Our clinical and experimental study is based on the evaluation of the changes in enzymatic activity produced by surgical, traumatic and infectious agression. To this end we have evaluated the activity of the transaminase (GOT-GPT), malic dehydrogenase (MDH), lactic dehydrogenase (LDH) and creatine phosphokinase (CPK). The details of our study are based on a total of 175 patients and 82 animals (dogs). Our results show that the highest rate of enzymatic activity was in proportion to the seriousness of the wound (lesion) produced. The clinical course-index developed from the activity of CPK and MDH allows us to evaluate and predetermine the course which our patients and our animals were to follow.
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PMID:[Alteration of serum enzyme activity after trauma and/or bacterial infection (author's transl)]. 44 61

We measured creatine kinase (EC 2.7.3.2) activity in 1009 serum samples from 538 patients in the intensive-care units of the University of Texas Medical Branch hospitals. Creatine kinase isoenzymes migrating cathodal to skeletal muscle creatine kinase (CK-MM) on cellulose acetate electrophoresis were found in sera from 14 of the 538 patients. Creatine kinase, lactate dehydrogenase (EC 1.1.1.27), aspartate aminotransferase (EC 2.6.1.1), and alanine aminotransferase (EC 2.6.1.2) activities were abnormally increased in these 14 patients. Liver lactate dehydrogenase isoenzyme (LDH5) and cardiac creatine kinase isoenzyme (CK-MB) were abnormally increased in 12 and eight of these patients, respectively. Ten of the 14 patients died during their hospital admission. We believe the creatine kinase isoenzymes that migrated cathodal to skeletal muscle creatine kinase (CK-MM) were of mitochondrial origin.
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PMID:Creatine kinase isoenzymes of mitochondrial origin in human serum. 44 29

In an experimental study, employing anaesthetized dogs, it was investigated whether cellular enzymes from peripheral skeletal muscle get into the circulating blood by diffusion across capillary membranes or by lymphatic transport. In the experimental group 1, the animals were anaesthetized only. The plasma activities of the four enzymes measured--lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, creatine kinase--did not show any mentionable change during a time period of 6 h. In group 2 one hind limb of each animal was moved passively for 1 h. Alanine aminotransferase remained unchanged in plasma, the activities of the three other enzymes increased significantly. In group 3 one hind limb was made hypoxic by clamping the femoral blood vessels for 1 h. No activity changes were observed. When the period of hypoxia was followed by a 1-hour period of passive movement in group 4, the alterations in plasma activities were almost identical to those observed in group 2. In group 5 the experimental procedure was as in group 4, in addition the lymph from the thoracic duct was quantitatively withdrawn. The enzyme activities in plasma revealed a tendency to decrease rather than increase. Lymph flow increased significantly as well as the lymphatic activities of those enzymes which have high intracellular activities in muscle. The results prove, that enzymes from muscle are transported from the interstitial into the intravascular compartment mainly by lymphatic transport. Indications were found that the interruption of blood flow in one hind limb did not result in an enzyme release from muscle cells. It is discussed how changes in lymph flow, occurring during physical exercise for example, affect enzyme activities in plasma.
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PMID:Lymphatic transport of cellular enzymes from muscle into the intravascular compartment. 45 37

Sets of survey specimens having known linear interralationships were analyzed on four occasions by approximately 450 laboratories for the five enzymes lactate dehydrogenase, aspartate aminotransferase, creatine kinase, alanine aminotransferase, and alkaline phosphatase. The results are summarized in terms of the apparent precision and relative accuracy of various analytical systems, and some apparent problems in enzyme assays are identified. The results show that interlaboratory differences in enzyme analyses are not due primarily to differences in the way laboratorians utilize their analytical systems but rather are due to fundamental differences in the instruments and reagents supplied to the laboratorians. The attainment of interlaboratory comparability of enzyme analyses is a problem that can best be addressed by the manufacturers of instruments and reagents, rather than by individual laboratorians.
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PMID:The 1978 College of American Pathologists survey of analyses of five serum enzymes by 450 laboratories. 47 5

The hypothesis that the prior intake of barbiturates may predispose patients to form increased amounts of oxalate following the intravenous infusion of xylitol was investigated in the rat. Phenobarbitone pre-treatment resulted in a 2-3 fold increase in urinary [14C] oxalate concentration following the intraperitoneal injection of [U-14C] xylitol or [l -14C] glycollate. The absence of any marked changes in urine volumes and creatinine excretion implied that this increase in urinary oxalate excretion was due to the enhanced synthesis of oxalate. The activities of key enzymes in hepatic oxalate synthesis, glycollate oxidase, lactate dehydrogenase, catalase and alanine aminotransferase were not altered by phenobarbitone pre-treatment. It is suggested that the increased activity of the microsomal mixed function oxidases, following phenobarbitone treatment, may facilitate the oxidation of glycollate and possibly xylitol. This communication leads experimental support to the concept that the prior intake of drugs, such as barbiturates, may predispose patients to form increased amounts of oxalate.
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PMID:Oxalate excretion in rats injected with xylitol or glycollate: stimulation by phenobarbitone pre-treatment. 48 83

In rats exposed for 12 weeks to the mixture of nitric oxides (0.34--2.81 mg/m3) and chlorine (0.61--1.50 mg/m3) the following changes were found: increased methemoglobin concentration (MetHb), increased partial pressure, increased total carbon dioxide concentration (pCO2 TCO2), increased current dicarbonate concentration (AB), and increased buffer bases (BB). In addition, asparagine transferase activity (aspAT), alanine aminotransferase (A1AT), alkaline phosphatase (AP) and hepatic isoenzyme of lactic dehydrogenase (LDH5) in serum were found to be increased. Histopathological examination revealed: inflammatory lesions and edema of pulmonary parenchyma, alveolar emphysema and edema of connective tissue of palpetra derm with mastocytes. Chronic exposure to low concentrations of nitric oxides and chlorine induces, apart from local lesions in conjunctivae, pulmonary lesions leading to respiratory acidosis compensated by metabolic alkalosis, or liberation of indicatory enzymes through impaired cells.
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PMID:[Chemical hazards connected with electrochemical machining. I. Toxicity of nitric oxides and chlorine lesions in rats' parenchymatous organs]. 50 41

Ceforanide, a new cephalosporin antibiotic with a long half-life (3 h), can be administered twice daily. We evaluated its antimicrobial activity, pharmacology, and clinical efficacy. Twenty-seven patients with infections due to susceptible organisms received ceforanide, 0.5, 1, or 2 g, intramuscularly or intravenously every 12 h for 6 to 28 days. In vitro studies with the clinical isolates from 27 patients treated plus 263 additional isolates showed that ceforanide was active against cephalothin-susceptible gram-positive and gram-negative microorganisms. In addition, ceforanide inhibited 65% of cephalothin-resistant Escherichia coli and 65% of Enterobacter spp. at </=12.5 mug/ml. After a single 1-g intramuscular dose, the mean peak plasma concentration at 1 h was 48.9 mug/ml and that at 12 h was 4.7 mug/ml. Plasma accumulation occurred in some patients. The infections included 10 pneumonias, 3 with bacteremia and 1 with empyema; 11 soft tissue infections, 4 with abscesses and 3 with sepsis; and 3 urinary tract infections. One case each of endocarditis, osteomyelitis, and septic thrombophlebitis, all due to Staphylococcus aureus, were treated. Clinical response was satisfactory in all patients; bacteriological response was satisfactory in 26 of 27 patients. Ceforanide was well tolerated. Three patients developed mild increases in liver enzymes, and one developed slight eosinophilia. In another case, the antibiotic was discontinued because of a fivefold rise in serum glutamic-oxalacetic transaminase (aspartate aminotransferase) and serum glutamic-pyruvic transaminase (alanine aminotransferase) and a twofold rise in lactic acid dehydrogenase and alkaline phosphatase.
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PMID:Ceforanide: in vitro and clinical evaluation. 50 95


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