Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.1 (aspartate aminotransferase)
 21,665 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In normal mongrel dogs, outflow occlusion of 15 or 30 minutes duration was produced by clamping both the suprahepatic and suprarenal portions of the vena cava. One dog died immediately after release of occlusion; two dogs died from recurrent hypotension between six and 24 hours postoperatively. The other five dogs survived for three days, at which time an autopsy was done. During outflow occlusion, the blood pressure fell in all dogs, as did the central venous pressure. The pulse rate decreased during, and after, occlusion but toward a tendency of gradual recovery. A significant drop in pH and base excess of arterial blood was seen after occlusion. Although a steady, but not substantial, increase in hemoglobin and hematocrit values was noted, there were no remarkable changes in the blood coagulation system. Significant increases in serum glutamic-oxalacetic transaminase, glutamic-pyruvic-transaminase, lactic dehydrogenase, acid phosphatase and beta-glucuronidase activities were observed from immediately after release of occlusion, but alkaline phosphatase values increased much later than did these. Thus, hepatic outflow occlusion, even if it is short, seems to be dangerous in the dog, since it produces hypotension, metabolic acidosis and diffuse damage as well as disruption of the parenchyma of the liver.
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PMID:Enzymatic and hemodynamic changes after short term hepatic outflow occlusion in the dog. 1 3

In experiments with albino rats it was found that after administration of phytobacteriomycin, trichotecin, hygromycin B or levoristatin into the stomach in doses of 1/20 of LD50 activity of the microsomal enzymes of the liver cells significantly changed and the changes persisted within at least 2 weeks. The above antibiotics induced similar changes in the lysosome enzyme, i.e. acid phosphatase, providing an increase in its activity. Changes in the activity of succinate dehydrogenase (mytochondria indicator enzyme), glucose-6-phosphatase (ribosome indicator enzyme) and aspartate aminotransferase (cytoplasm indicator enzyme) were different for each antibiotic. It is concluded that the above antibiotics were capable of impairing on intoxication the enzymatic function of various cell microstructures, though the levels of the change direction may be different.
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PMID:[Effect of phytobacteriomycin, trichotecin, hygromycin B and levoristatin on some rat liver enzymes]. 5 75

The effect of N6,O2'-dibutyryl adenosine 3',5'-cyclic-monophosphate (dbcAMP) on the mobilization of calcium (Ca2+), inorganic phosphate (Pi) and lysosomal enzymes was studied in a bone culture system for 24 h using half calvaria from 6--7 day-old mice. DbcAMP inhibited spontaneous as well as parathyroid hormone-stimulated mineral mobilization. DbcAMP in a concentration of 5 x 10(-4)M also reduced the activities of beta-glucuronidase, beta-galactosidase and acid phosphatase found in the media while the activities of lactate dehydrogenase, aspartate aminotransferase and alanine aminotransferase were not affected. It is concluded that cAMP is not a stimulator but an inhibitor of bone resorption within the culture period studied (24 h) and that the cyclic nucleotide might interfere with release processes involved in bone resorption.
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PMID:Inhibitory effect of dibutyryl cyclic AMP on the release of calcium, inorganic phosphate and lysosomal enzymes from calvarial bones cultured for 24 hours. 22 6

Kadazans, the largest indigenous group in Sabah, northern Borneo, were surveyed for glyoxalase I, phosphoglucomutase I, red cell acid phosphatase, esterase D, adenosine deaminase, soluble glutamate pyruvate transaminase, soluble glutamate oxaloacetate transaminase, 6-phosphogluconate dehydrogenase, uridine monophosphate kinase, adenylate kinase, peptidase B and D, superoxide dismutase, C5, group specific component, haptoglobin and transferrin. Kadazans were found to be polymorphic for GLO I, PGM I, RCAP, esterase D, ADA, s-Gpt, 6PGD, UMPK, Gc, C5, haptoglobin and peptidase B. Rare variants were found for transferrin and peptidase D. No variant was found for s-Got, SOD and AK.
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PMID:Biochemical genetic markers in the Kadazans of Sabah, Malaysia. 28 26

1. Enzyme activities were studied in blood plasma from Rhenish, Italian, Landes and Masseubian geese. 2. Strains used for liver production (Landes, Masseubian) showed higher activities of aspartate transaminase (AST) [EC 2.6.1.1], alanine transaminase (ALT) [EC 2.6.1.2] and fructose aldolase (FRA) [EC 4.1.2.13] while breeds with high egg production (Rhenish, Italian) had higher activities of both alkaline phosphatase (ALP) [EC 3.1.3.1] and acid phosphatase (ACP) [EC 3.1.3.2]
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PMID:Blood enzyme activities in different breeds of geese. 49 70

The results of sending specimens through a computerized pneumatic airtransport system and manually delivering specimens were compared for 15 chemical tests and six hematologic procedures. All specimens were collected from inpatients and outpatients into evacuated glass containers. The specimens traversed a maximum of 829 feet (253 meters) involving 16 bends and eight transfer units at 25 feet/second (7.6 meters/second). Only the activity of lactate dehydrogenase exceeded the precision of the test in pneumatically transported specimens. Ruptured erythrocytes in incompletely filled vacuum tubes were the likely source of the increased lactate dehydrogenase activity. Neither the serum sodium, potassium, chloride, carbon dioxide, total protein, albumin, calcium, glucose, creatinine, total bilirubin, alkaline phosphatase, aspartate transaminase, acid phosphatase, uric acid, leukocyte count, erythrocyte count, hemoglobin, hematocrit, nor the prothrombin time and partial thromboplastin time were affected by pneumatic transport. It is concluded that the pneumatic system tested provides a safe, efficient method of transporting the blood specimens tested.
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PMID:Evaluation of a computer-directed pneumatic-tube system for pneumatic transport of blood specimens. 70 6

Lactic dehydrogenase (LDH), glutamic-oxalacetic transaminase (GOT), and acid and alkaline phosphatase activities in bone marrow and in cubital vein serum were compared. For patients without cancer, marrow serum LDH attained levels four times as high, and GOT and alkaline phosphatase, levels twice as high as those normal for cubital vein serum; levels of acid phosphatase were the same for both sources. For patients with cancer, significant increase of enzyme levels over reference levels depends on the tumor origin and on the presence and localization of metastases. Marrow enzyme levels may become elevated with or without concurrent elevation in cubital vein serum. Concurrent elevations were found with colonic carcinoma and lymphoid leukemia, and noncurrent elevations, with prostatic cancer, myeloid leukemia, and myeloma. A nonconcurrent elevation of marrow enzymes indicates that the origin of the enzyme is in the marrow, whereas with concurrent elevation, the source of the enzyme may be another organ.
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PMID:Enzymes in peripheral and bone marrow serum in patients with cancer. 98 36

In women employed in an industrial plant in direct contact with epoxide resins and their hardeners, the following biochemical parameters were determined in blood: total protein, seromucoid, haptoglobin, hemoglobin variants, methemoglobin, alpha1-inhibitor of trypsin, lactate dehydrogenase, aspartate and alanine aminotransferases, alkaline and acid phosphatase, gamma-glutamyl transpeptidase, leucylaminopeptidase, and alanine aminopeptidase. Depending on duration of work, Hb A2 fraction and lactate dehydrogenase increased significantly, and aspartate aminotransferase, acid and alkaline phosphatase activities decreased. In pregnant women, leucylaminopeptidase activity and isozyme of placental alkaline phosphatase were decreased.
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PMID:Evaluation of the influence of epoxide resins and their hardeners on the female body. II. Biochemical studies. 101 94

The activities of aspartate transminase (EC 2.6.1.1), alanine transminase (EC 2.6.1.2), alkaline phosphatase (EC 3.1.3.1), acid phosphatase (EC 3.1.3.2) leucine arylamidase (EC 3.4.1.1), aldolase (EC 4.1.2), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.38) and cholinesterase (EC 3.1.1.7) were measured in serum of male rabbits and albino Wistar rats in dlplicate by means of microliter techniques. Furthermore, the diurnal alterations of enzyme activity were established in 8--10 animals of both species. Aspartate transaminase activity in the serum of rats was found to be significantly higher than in the serum of humans and rabbits, and essentially lower alkaline phosphatase values were obtained from the serum of rabbits in comparison with those found for the serum of humans and rats. Relatively high acid phosphatase and aldolase values as well as a very low cholinesterase activity were found in the serum of rabbits and rats. The mean malate dehydrogenase-activity was found to be twice as high as the mean lactate dehydrogenase, which is the contrary of the situation found in human serum. No significant diural alterations of the examined enzyme activities were established. The differences found between the animal and the human enzyme activities in serum are explained by species-determined peculiarities of metabolism or specific enzyme configuration.
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PMID:[Enzyme activities in serum of rabbits and rats-reference values and circadian alterations. Serum enzymes and factors that influence their activity,I (AUTHOR'S TRANSL)]. 103 68

Changes in protein elution patterns and among others in the distribution profiles of some isozymes, as the lysosomal acid phosphatase, the microsomal alkaline phosphatase, the cytoplasmic fraction of aspartate aminotransferase and some fractions of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, have been found in liver experimental fatty change induced in rats by carbon tetrachloride and ethionine. The possible meaning of these changes is discussed.
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PMID:Rat liver isozymes in acute carbon tetrachloride and ethionine poisoning. 112 37


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