Results 201 to 210 of about 13,961 (264)

Hypertransaminasemia Is a Marker of Severity in Children Hospitalized for Influenza. [PDF]

open access: yesInfluenza Other Respir Viruses
Poeta M   +17 more
europepmc   +1 more source

Discovery of the protective effect of glutamine on acute alcoholic liver injury.

open access: yesIndian J Pharmacol
Yang H   +6 more
europepmc   +1 more source
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Evolutionary analysis of aspartate aminotransferases

Journal of Molecular Evolution, 1995
Aspartate 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.
Chris Winefield   +2 more
exaly   +3 more sources

Measurement of Aminotransferases: Part 1. Aspartate Aminotransferase

CRC Critical Reviews in Clinical Laboratory Sciences, 1984
Aminotransferases 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
exaly   +3 more sources

Macromolecular aspartate aminotransferase

European Journal of Gastroenterology & Hepatology, 1998
Macroenzymes 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
openaire   +2 more sources

Aminotransferases in Grapes. Isolation and Characterization of Aspartate Aminotransferase

American Journal of Enology and Viticulture, 1991
International ...
Sauvage, F.X.   +3 more
openaire   +2 more sources

Buffers for the reconstitution of aspartate aminotransferase

Biochemical and Biophysical Research Communications, 1988
The cofactor activation of the apoenzyme of pig heart cytosolic aspartate aminotransferase was studied in various buffers. Cationic buffers are shown to allow maximal reconstitution in the pH range of 5.0 to 9.0. Anionic buffers made up of mono- and dicarboxylates are found to affect reconstitution in a pH-dependent manner.
J L, Lambing   +5 more
openaire   +2 more sources

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