Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Biochemical method was adopted to examine 10 kinds of histologic enzyme spectrum activities in gastric intestinal metaplasia, carcinoma and normal or superficial gastritis mucosa taken from different sites from 17 fresh surgical specimens of stomach. The enzymes are aldolase (ALD), pyruvate kinase (PYK), phospho hexo-isomerase (PHI), lactic dehydrogenase (LDH), creatine phosphokinase (CPK), hydroxybutyrate dehydrogenase (HBD), glutamic-pyruvic transaminase (GPT), alkaline phosphatase (AKP), acid phosphatase (ACP), r-glutamyl-transpeptidase (gamma-GT). Among glycolytic enzymes the content of ALD, PYK in intestinal metaplasia were 24.5 u and 24.6 u respectively, which were higher than those in the normal mucosa (15.7, 18.0) and lower than carcinoma (28.4, 29.6) (P less than 0.01-0.05). The content of CPK in intestinal metaplasia was lower (218.5 u) than that in the normal (463.9 u) and higher than that in carcinoma (110.3 u) (P less than 0.01). Among protease and amino acid enzymes the content of HBD in intestinal metaplasia was lower (108.2 u) than those in the normal (221.3 u) and carcinoma (113.9 u) (P less than 0.05). The content of GPT in intestinal metaplasia was (6.7 u) which was lower than that in the normal (9.4 u) and higher than that in carcinoma (3.7 u) (P less than 0.01). The above results could provide reference indices for judging the potential malignancy of gastric intestinal metaplasia.
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PMID:[Relationship between gastric carcinoma and enzyme spectrum activity in gastric mucosal intestinal metaplasia]. 161 87

The activity of lactate dehydrogenase (LDH), indophenol oxidase, aspartate aminotransferase (AsAT), alkaline phosphatase, acid phosphatase and aldolase at different stages of rat development was measured. We have also determined changes in the activity of these enzymes resulting from transplantation of embryonic nerve tissue (ENT) into the brain of adult animals. During development from the embryo to the adult animal, LDH and AsAT activities increased, while alkaline phosphatase activity diminished. After ENT transplantation, the most prominent changes were in the alkaline phosphatase activity whereas the activity of LDH, AsAT and acid phosphatase remained unchanged and similar to that in the brain cortex of intact adult animals. Changes in the enzyme activity resulting from ENT transplantation changed in a manner characteristic of the transplant. Local brain damage did not change the activity of the studied enzymes fifty days after surgery.
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PMID:[Changes in the activity of different classes of enzymes in the cerebral cortex of rats in ontogeny and after the transplantation of embryonic nerve tissue]. 223 89

Rabbit skeletal muscle and liver fructose 1,6-diphosphate aldolases autophosphorylate in the presence of inorganic phosphate at physiological and alkaline pH. ATP as well as nonhydrolyzable ATP analogues inhibits autophosphorylation. Autophosphorylation of aldolases abolishes catalytic activity, which is restored upon treatment with alkaline phosphatase. Limited proteolysis of aldolase preferentially hydrolyzes the COOH terminus and liberates a phosphorylated peptide. Treatment of rabbit aldolases with carboxypeptidase, which liberates the COOH terminal residue Tyr 363, although modifying catalytic activity does not affect autophosphorylation. Amino acid analyses are consistent with results of autophosphorylation of the COOH terminus showing residue His 361 in muscle aldolase and Tyr 361 in liver aldolase. Phosphate lability in acid pH by phosphorylated muscle aldolase but not by phosphorylated liver aldolase corroborates the amino acid assignment. Autophosphorylation of the aldolases in the crystalline state is consistent with an intramolecular mechanism. The pH dependence of autophosphorylation being dependent on the enzyme's physical state (soluble or crystalline) is not inconsistent with crystallization stabilizing a conformer having different amino acid pka values and/or reactivities than those of the soluble state.
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PMID:Inactivation of mammalian fructose diphosphate aldolases by COOH terminus autophosphorylation. 227 41

Elevated levels of serum enzymes are frequently associated not only with alcohol-related organ damage but also with excessive alcohol consumption and alcoholism without significant tissue injury. However, both in the early detection of alcoholism as well as also in the diagnosis of alcohol-related diseases the sensitivities and specificities of these enzyme markers vary considerably. They may be influenced by nonalcohol-related diseases, enzyme-inducing drugs, nutritional factors, metabolic disorders, age, smoking, etc. Consequently, we have neither a single laboratory test--enzyme marker--nor a test combination that is reliable enough for the exact diagnosis between alcohol- and nonalcohol-related organ damage. In most cases it is possible to determine the tissue from which the elevated enzyme is derived, but only occasionally enzyme changes reflect the quantity of the tissue injury. Gamma-glutamyltransferase (GGT) is the most widely used laboratory marker of alcoholism and heavy drinking, detecting 34-85% of problem drinkers and alcoholics. However, the unspecificity of increased serum GGT limits its use for general screening purposes. Its value in the follow-up of various treatment programs, however, is well established. An elevated level of serum aspartate aminotransferase (ASAT) and alanine aminotransferase (ALAT) in an alcoholic or a heavy consumer indicates alcohol-induced organ damage. The use of test combinations significantly improves the information received with single serum enzyme determinations. An ASAT/ALAT ratio greater than 1.5 can be considered as highly suggestive for the alcoholic etiology of the liver injury. Still better discrimination between alcoholic and nonalcoholic origin of the liver disease may be achieved by the determination of the ratio of GGT to alkaline phosphatase. If this ratio exceeds 1.4 the specificity of the finding in favor for alcoholic liver injury is 78%. The determination of the mitochondrial isoenzyme of ASAT also improves the diagnostic value of ASAT determination. The ratio of mitochondrial isoenzyme to total over 4 is highly suggestive for alcohol-related liver injury. In general, however, the determination of serum activities of other enzymes such as ornithine carbamyl transferase, lactate dehydrogenase, isocitrate dehydrogenase, sorbitol dehydrogenase, alcohol dehydrogenase, guanase, aldolase, alkaline phosphatase or glutathione S-transferase do not significantly improve the diagnostic information obtained with more conventional laboratory markers of liver injury.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Use of enzymes for the diagnosis of alcohol-related organ damage. 243 6

Dietary hexachlorocyclohexane (HCH) and gamma-isomer of HCH produced significant increase in liver weights of mice. Elevated levels of alanine and aspartate aminotransferases and of alkaline phosphatase in the blood of these animals suggested hepatotoxicity. Hepatic soluble enzymes--aspartate aminotransferase and lactate dehydrogenase--were markedly lowered. Among the hepatic lysosomal enzymes, acid phosphatase and acid cathepsin were increased in the experimental animals. Hepatic glucose-6-phosphatase was lowered by HCH while aldolase activity was increased. Hydrolytic enzymes in small intestine, viz., disaccharidases, lipase, amylase, dipeptidase and phosphatases, were also affected by dietary HCH and gamma-HCH. The results suggested cellular toxicity in hepatocytes of HCH and gamma-HCH fed animals, and also interference in gastrointestinal absorption.
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PMID:Biochemical toxicity of hexachlorocyclohexane and its gamma-isomer in albino mice. 248 47

A comparative trial was conducted with the oral administration of zinc sulphate to pregnant cows and heifers aimed at influencing the selected metabolic parameters in the dam-calf line. The total daily ZnSO4.7H2O dose of 3 g (680 mg Zn++) was given to dry standing cows and heifers for 35 days on an average (15-65) before the expected date of calving. The breeding conditions in the stock were problematic: losses of calves suffered in the last half-a-year period were higher than 30% of born calves; the main causes of this high mortality were coli-septicaemia and coli-enteritis. As compared with the eight control animals, the experimental cows and heifers (12 head) exhibited a transient increase in zincaemia, followed by a tendency to proteinaemia; aspartate aminotransferase activity increased, total immunoglobulins remained unchanged, and decreases were recorded in the activities of alanine aminotransferase, alkaline phosphatase, creatine phosphokinase and aldolase. On the other hand, the concentration of total bilirubin tended to increase. In 77% of the cows and first-calvers of the experimental group the quality of colostrum complied with the standard; in the case of the control animals this proportion was 83%. Significant zincaemia occurred in the calves of the experimental cows between the first and 14th day of their age; no differences from the control calves were recorded in immunoglobulinaemia, proteinaemia, albuminaemia and in the activities of alanine aminotransferase and creatine phosphokinase. On the other hand, aspartate aminotransferase activity tended to grow and alkaline phosphatase activity tended to sink. Neonatal hyperbilirubinaemia disappeared within the first 14 days of age in both the experimental and the control calves. The results failed to show clearly that the intention to increase the values of the studied parameters of immunopoiesis was met.
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PMID:[Peroral administration of zinc sulfate to pregnant cows and its effect on selected metabolic indicators in the dam-calf lineage]. 273 89

Ten male Holstein-Friesian calves naturally infected by Mycobacterium paratuberculosis were experimentally re-infected orally at an average of 17 days. Monthly measurements were conduced of the following activities, in the period between post infection days 160 and 400: total protein (TPR), albumin (ALB), cholesterol (CHOL), triglycerides (TRIG), Zn and Cu concentrations as well as sorbitol dehydrogenase, lactate dehydrogenase (LDH), alpha-hydroxybutyrate dehydrogenase (alpha-HBDH), gamma-glutamyltransferase, aspartate aminotransferase (AST), alanine aminotransferase (ALT), creatine kinase (CK), alkaline phosphatase and fructose-1,6-diphosphate aldolase (ALD). TPR, ALB, TRIG, and CHOL were reduced by day 400, in conjunction with disorders of digestion and absorption. Increased activities of CK, ALD, LDH, alpha-HBDH, AST and ALT primarily indicated damage to skeletal muscle and/or liver. Serum CK and ALD activities as well as TRIG and TPR concentrations may serve as aids to specific diagnosis of paratuberculosis, particularly in the advanced stage of the disease.
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PMID:Experimental paratuberculosis (Johne's disease)--studies on biochemical parameters in cattle. 277 44

The effects of recombinant human interleukin-1 beta (rhIL-1 beta) on various serum constituents were studied following subcutaneous injection (12.5 or 125 micrograms/kg) in female Wistar rats. Protein electrophoresis and the determination of the serum concentrations of carboxypeptidase N (CPN), aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, aldolase, total proteins, iron, urea, creatinine, and several amino acids were performed 12, 24, and 72 hr after injection. With both doses of rhIL-1 beta, iron, albumin, CPN, and lysine were significantly decreased whereas alpha 2-globulin, urea, and creatinine were significantly increased 12 hr after administration. Iron and CPN were still low after 24 hr but returned to normal levels after 72 hr. With the higher dose of rhIL-1 beta, only alanine and phenylalanine levels were increased after 12 and 72 hr, taurine after 12 hr, and methionine after 24 hr. There were no biochemical or histological signs of hepatotoxicity. The findings indicate that rhIL-1 beta produces a reversible alteration of various biochemical plasma constituents without any apparent signs of cytotoxicity. Moreover, the decrease in CPN observed may influence the degradation of inflammatory peptides.
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PMID:Recombinant human interleukin-1 beta decreases serum carboxypeptidase N and modifies serum amino acid concentrations in rats. 278 29

The stability and storage characteristics were studied of 11 bovine enzymes of potential clinical significance, namely, aldolase, alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase, acetylcholinesterase, creatine kinase, gamma glutamyltransferase, glutathione peroxidase (GSH-Px), alpha-hydroxybutyrate dehydrogenase, lactate dehydrogenase and superoxide dismutase (SOD). Enzyme activities in fresh serum were compared with those in plasma containing various anticoagulants including lithium heparin, EDTA and oxalate/fluoride. The same preservatives were assessed for their effects on the whole blood activities of GSH-Px and SOD. Stabilities of enzymes in plasma and serum stored at room (+20 degrees C), refrigerator (4 degrees C) or deep freeze (-20 degrees C) temperatures were also compared. In addition, SOD and GSH-Px activities in samples stored, at the same temperatures, as whole blood or aqueous lysates were monitored.
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PMID:Stability and storage characteristics of enzymes in cattle blood. 286 28

The stability and storage characteristics were studied of 11 ovine enzymes of potential clinical significance, namely, aldolase, alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase, acetylcholinesterase, creatine kinase, gamma glutamyltransferase, glutathione peroxidase (GSH-Px), alpha-hydroxybutyrate dehydrogenase, lactate dehydrogenase and superoxide dismutase (SOD). Enzyme activities in fresh serum were compared with those in plasma containing various anticoagulants including lithium heparin, EDTA and oxalate/fluoride. The same preservatives were assessed for their effects on the whole blood activities of GSH-Px and SOD. Stabilities of enzymes in plasma and serum stored at room (+20 degrees C), refrigerator (4 degrees C) or deep freeze (-20 degrees C) temperatures were also compared. In addition, SOD and GSH-Px activities in samples stored, at the same temperatures, as whole blood or aqueous lysates were monitored. The results are discussed with particular reference to the differences between sheep and cattle.
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PMID:Stability and storage characteristics of enzymes in sheep blood. 286 29


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