Results 261 to 270 of about 16,662 (295)
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Macromolecular aspartate aminotransferase
European Journal of Gastroenterology & Hepatology, 1998Macroenzymes are serum enzymes that have a greater molecular mass than the corresponding enzyme normally found in serum (Klonoff. West J Med 1980; 133: 392-407). Serum AST (aspartate aminotransferase) has rarely been reported to complex with immunoglobulins, resulting in an elevation in serum AST activity.
J, Tharakan, A, Hossenbocus, M J, Arthur
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Aspartate aminotransferase ofLactobacillus murinus
Folia Microbiologica, 1988Aspartate aminotransferase from Lactobacillus murinus is thermostable, its activity being not changed for two months at temperatures between 4 and -70 degrees C. Maximum activity was observed at 40 degrees C and pH 7.3 in phosphate buffer (30 mmol/L). delta G* Value of 26.3 kJ/mol was calculated from the Arrhenius plot.
G, Rollan +3 more
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Measurement of Aminotransferases: Part 1. Aspartate Aminotransferase
CRC Critical Reviews in Clinical Laboratory Sciences, 1984Aminotransferases are ubiquitous enzymes of mammalian cells and several are of important diagnostic use. The application of aspartate aminotransferase activity measurements in serum from individuals suffering from myocardial infarction brought about a new dimension in clinical laboratory testing in the 1950s.
Robert Rej, Leslie M. Shaw
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Aspartate aminotransferase isoenzymes
Clinical Biochemistry, 1990Aspartate aminotransferase (AST, EC 2.6.1.1) exists in human tissues as two distinct isoenzymes, one located in the cytoplasm (c-AST), and the other in mitochondria (m-AST). Striated muscle, myocardium, and liver tissues are the main sources of AST. A growing body of information suggests that determination of AST isoenzymes in human serum is useful in ...
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Evolutionary analysis of aspartate aminotransferases
Journal of Molecular Evolution, 1995Aspartate aminotransferase isoenzymes are located in both the cytosol and organelles of eukaryotes, but all are encoded in the nuclear genome. In the work described here, a phylogenetic analysis was made of aspartate aminotransferases from plants, animals, yeast, and a number of bacteria.
C S, Winefield +3 more
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Reconstituted aspartate aminotransferase physical studies
Biochimica et Biophysica Acta (BBA) - Enzymology, 1968Abstract Apo-aspartate aminotransferase ( l -aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from pig heart can be recombined with pyridoxal 5-phosphate to form reconstituted species with properties indistinguishable from those of the original enzyme. Two distinct types of enzyme properties were investigated in these studies.
J G, Farrelly, J E, Churchich
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Macro-aspartate aminotransferase and pregnancy
European Journal of Gastroenterology & Hepatology, 2004Macro-aspartate aminotransferase (AST) is a benign condition characterised by unexplained persistent fluctuations f this macroenzyme complex in serum. However, it is not clear what causes this phenomenon or which factors favour its appearance in the blood. Moreaover, it is not known whether normal pregnancy mayinfluence macro-AST levels or whether this
ORLANDO, ROCCO, LIRUSSI F.
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Inhibition of aspartate aminotransferase by hydrazinosuccinate
Biochimica et Biophysica Acta (BBA) - General Subjects, 1984DL-Hydrazinosuccinic acid was synthesized by the reaction of DL-bromosuccinic acid with hydrazine. The compound strongly inhibited aspartate aminotransferase and gave 50% inhibition at 1.3 microM when added simultaneously with L-aspartate to an assay mixture containing enzyme. Incubation of the enzyme with the compound prior to assay resulted in a much
R H, Yamada +3 more
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Essential arginyl residues in aspartate aminotransferases
Biochemical and Biophysical Research Communications, 1975Summary The active sites of the aspartate aminotransferases from both pig heart supernate and beef kidney mitochondria contain functional arginyl residues. Inactivation with butanedione in the presence of borate buffer, its reversal by gel filtration and irreversible inactivation with phenylglyoxal provide strong evidence for a functional role of ...
J F, Riordan, R, Scandurra
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