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beta glucuronidase/infarto
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Página 1 a partir de 34 resultados
Serum and urinary beta-galactosidase and beta-glucuronidase activity in patients with acute myocardial infarction.
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To determine the effect of acute myocardial infarction (AMI) on serum and urinary activity of beta-galactosidase and beta-glucuronidase (lysosomal enzymes) 40 patients were studied. Eighteen patients had acute myocardial infarction and 22 were assigned as controls. Three of the 18 patients with
[Behavior of the histochemically demonstrable activity of beta-glucuronidase in experimental myocardial infarct of the rat].
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Morphology and mitochondrial function of the surviving myocardium following myocardial infarction in the cat.
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The surviving myocardium of the cat was studied 7 days and 6 weeks following experimental infarction. Seven days after infarction, ultrastructural alterations of the mitochondria indicative of slight hypoxic injury--clearing of the matrix and loss of dense matrix granules--were found. Together with
Plasma lysosomal enzyme activity in acute myocardial infarction.
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N-acetyl-beta-glucosaminidase (EC 3.2.1.30, recommended name beta-N-Acetylglucosaminidase) was found to be a constituent of human cardiac lysosomes. beta-glucuronidase was also found in this tissue, while lysozyme, an enzyme present in leucocyte lysosomes, was not detectable in the heart. The
Plasma lysosomal enzyme activity in acute myocardial infarction and the effects of drugs.
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The activity of N-acetyl-beta-glucosaminidase (NAG) was found to be increased in serial plasma samples from patients with acute myocardial infarction (AMI). Maximum activity occurred 18 hr after the onset of chest pain, and a further peak of activity was found at 72 hr. Four isozymes of NAG were
Antilipoperoxidative and membrane stabilizing effect of diosgenin, in experimentally induced myocardial infarction.
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Altered membrane integrity has been suggested as a major factor in the development of cellular injury during myocardial necrosis. The present study was designed to investigate the effect of diosgenin on lysosomal hydrolases, membrane-bound enzymes, and electrolytes during isoproterenol (ISO)-induced
Arbutin prevents alterations in mitochondrial and lysosomal enzymes in isoproterenol-induced myocardial infarction: An in vivo study
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The present study demonstrated the protective effects of arbutin (ARB) on hyperlipidemia, mitochondrial, and lysosomal membrane damage and on the DNA damage in rats with isoproterenol (ISO)-induced myocardial infarction (MI). Rats were pretreated with ARB (25 and 50 mg/kg body weight (bw)) for 21
Influence of isoproterenol-induced myocardial infarction on certain glycohydrolases and cathepsins in rats.
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The changes in the activities of certain lysosomal hydrolases, viz., beta-glucuronidase, beta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, alpha-mannosidase, cathepsin B, cathepsin D, and collagenolytic cathepsin, in serum and heart of rats
[Histochemical studies of neutrophils in myocardial infarct patients].
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Cytochemical assays of neutrophil acid phosphatase, beta-glucuronidase, N-acetyl-beta-D-glycosamidase (NAG), myeloperoxidase activities, and the Sudan black B test, were carried out in 25 patients with myocardial infarction. Leucocytosis seen in the early days of infarction was associated with
Lysosomes in myocardial infarction: studies by means of cytochemistry and subcellular fractionation, with observations on the effects of methylprednisolone.
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To evaluate lysosomal involvement in myocardial infarction, coronary artery thrombosis was induced by ligation in 16 dogs. Biopsies of infarcted and normal left ventricles were studied by ultrastructural cytochemistry and subcellular fractionation (0.25 M sucrose) from 30 min to 96 hrs post injury.
(-) Epicatechin prevents alterations in lysosomal glycohydrolases, cathepsins and reduces myocardial infarct size in isoproterenol-induced myocardial infarcted rats.
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The preventive effects of (-) epicatechin on oxidative stress, cardiac mitochondrial damage, altered membrane bound adenosine triphosphatases and minerals were reported previously in isoproterenol-induced myocardial infarction model. Leakage of lysosomal glycohydrolases and cathepsins play an
Alterations in the heart lysosomal stability in isoproterenol induced myocardial infarction in rats.
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The alterations in the heart lysosomal stability following isoproterenol induced myocardial infarction were studied in albino rats. The rate of release of beta-glucuronidase at various time intervals at 37 degrees C from lysosome rich fraction was taken as a measure of lysosomal stability. As
Synergistic effect of nicorandil and amlodipine on lysosomal hydrolases during experimental myocardial infarction in rats.
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The synergistic effect of nicorandil (K(ATP) channel opener) and amlodipine (calcium channel blocker) on lysosomal hydrolases in serum and heart was examined by determining the activity of beta-glucuronidase, beta-N-acetyl glucosaminidase, beta-galactosidase, cathepsin-D and acid phosphatase on
Preventive effect of naringin on cardiac markers, electrocardiographic patterns and lysosomal hydrolases in normal and isoproterenol-induced myocardial infarction in Wistar rats.
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Diets rich in natural antioxidants are associated with reduced risk of heart diseases. This study was aimed to evaluate the preventive role of naringin on cardiac troponin T (cTnT), lactate dehydrogenase (LDH)-isoenzyme, cardiac marker enzymes, electrocardiographic (ECG)-patterns and lysosomal
Protective role of curcumin against isoproterenol induced myocardial infarction in rats.
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The effect of curcumin on the biochemical changes induced by isoproterenol (ISO) administration in rats was examined. ISO (300 mg Kg-1 administered subcutaneously twice at an interval of 24 h) caused a decrease in body weight and an increase in heart weight, water content as well as in the levels of
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