Results 261 to 270 of about 23,342 (303)
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CEREBRAL AROMATIC AMINOTRANSFERASE

Journal of Neurochemistry, 1975
Abstract—Aromatic: 2‐oxoglutarate aminotransferase has been purified about 950‐fold from rat brain mitochondria. The purified enzyme was homogeneous in polyacrylamide gel electrophoresis and had a molecular weight of approx 63,000. On the basis of substrate specificity, substrate inhibition, purification ratio, yield, polyacrylamide gel electrophoresis
T, Noguchi   +4 more
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Redesign of aspartate aminotransferase specificity to that of tyrosine aminotransferase

1994
The values of kcat/Km are strongly correlated with chain length for the reactions of E. coli tyrosine aminotransferase, but are nearly independent of this variable for aspartate aminotransferase. Both enzymes exhibit nearly equal reactivity with dicarboxylic acid substrates.
Jack F. Kirsch, James J. Onuffer
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Comparison of aspartate aminotransferase with other aminotransferases by absorption-spectrum analysis

Biochemical Society Transactions, 1984
Gehring, H. & Christen, P. (1978) J. Biol. Chem. 253, 3158-3163 Gehring, H., Sandmeier, E., Kirsten, H., Carrassi, R., Christen, P. & Jansonius, J . N. (1984) in Biological Asoects of Vitamin &, Catalysis (Evangelopoulos, A. E., ed.), Alan R. Liss, New York, in the press Graf-Hausner, U., Wilson, K. J. & Christen, P. (1983) J. Biol. Chem.
R A, John, P H, Morgan, L J, Fowler
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Evolutionary and Biosynthetic Aspects of Aspartate Aminotransferase Isoenzymes and Other Aminotransferases

Annals of the New York Academy of Sciences, 1990
The mitochondrial and cytosolic isoenzymes of aspartate aminotransferase are homologous proteins. Both are encoded by nuclear DNA and synthesized on free polysomes. The organization of their genes is very similar, five out of a total of eight introns are located at the same nucleotide position. A variant consensus sequence was observed at the 3' splice
Christen P   +5 more
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Aspartate aminotransferase isoenzymes

Clinical Biochemistry, 1990
Aspartate 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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Elevated Serum Aminotransferases

JAMA, 2022
Kristel K, Leung, Gideon M, Hirschfield
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Kynurenine Aminotransferase in Hypercholesterolemic Rats

1996
Nicotinic acid is used in the treatment of atherosclerosis for its hypolipidemic effects (Kritchevsky, 1971; Levy, 1980; Grundy et al., 1981; Altschul et al., 1995), which reduce triglycerides and also cholesterol. In mammals, nicotinic acid derives from the metabolism of tryptophan along the kynurenine pathway.
BERTAZZO, ANTONELLA   +5 more
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Stability of aspartate aminotransferase and alanine aminotransferase activities.

The Journal of laboratory and clinical medicine, 1983
Because there are conflicting data regarding the effect of different temperatures and durations of storage on the stability of the activities of aspartate aminotransferase (AST) and alanine aminotransferase (ALT), a new study has been conducted to re-examine this important issue.
B, Cuccherini   +4 more
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[Increase of aminotransferases].

La Revue de medecine interne, 1994
Elevated aminotransferases activities are frequent in medical practice. In acute elevations, the mains causes are generally easily found (viral, drug-induced, toxic, ischemic). In moderate or prolonged elevations, the most frequent causes are steatosis (alcoholic, diabetes, obesity) and chronic hepatitis (viral B, D, C, drug-induced and auto-immune ...
C, Trivalle   +7 more
openaire   +1 more source

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