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Valproate-induced hyperammonemic encephalopathy after aneurysm clipping surgery: a case report with literature review. [PDF]
Front Med (Lausanne)Liu M, Sang T, Lu X, Li B.
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Clinical Chemistry and Laboratory Medicine (CCLM), 2013
Abstract Background: Alanine aminotransferase (ALT), aspartate aminotransferase (AST) and γ-glutamyl transferase (GGT) are enzymes measured in serum or plasma to investigate liver disease. The aim of this work is to assess the validity of published biological variation (BV) data currently available for these enzymes.
A. Carobene +4 more
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Abstract Background: Alanine aminotransferase (ALT), aspartate aminotransferase (AST) and γ-glutamyl transferase (GGT) are enzymes measured in serum or plasma to investigate liver disease. The aim of this work is to assess the validity of published biological variation (BV) data currently available for these enzymes.
A. Carobene +4 more
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Natural Toxins, 1998
The effect of three forms pyoverdin on mouse liver was studied. Significant increases of alanine amino transferase (ALT) and aspartate amino transferase (AST) were obtained in mice after ingestion of water with forms A and C. The effect on liver was more evident with A than with C. Pyoverdin was purified by means of salt saturation, solvent extractions
A J, Eraso, I, Albesa
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The effect of three forms pyoverdin on mouse liver was studied. Significant increases of alanine amino transferase (ALT) and aspartate amino transferase (AST) were obtained in mice after ingestion of water with forms A and C. The effect on liver was more evident with A than with C. Pyoverdin was purified by means of salt saturation, solvent extractions
A J, Eraso, I, Albesa
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Regulation of aspartate amino-transferase isozymes by glyceraldehyde-3-phosphate
Advances in Enzyme Regulation, 1972Abstract This review concerns our work on glyceraldehyde-3-P as a time-dependent inhibitor of rat liver aspartate aminotransferase isozymes, and the possibility that glyceraldehyde-3-P may function as a rapidly acting regulator of aspartate aminotransferase.
J S, Nisselbaum +2 more
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Complete primary structure of cytoplasmatic aspartate-amino transferase from hog heart muscle
Bulletin of the Academy of Sciences of the USSR Division of Chemical Science, 1974The complete amino acid sequence of the cytoplasmatic aspartate-amino transferase from hog heart muscle was established. The enzyme consists of two identical subunits, each of which represents one polypeptide chain that contains 412 amino acid residues. The molecular weight of one aspartate-amino transferase subunit is 46, 344.
Yu. A. Ovchinnikov +11 more
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Developmental Biology, 1976
Abstract Activities of enzymes in the de novo pathway, aspartate carbamyl transferase, and salvage pathway, thymidine and uridine kinases, for nucleotide precursor synthesis were examined under conditions of innervation and denervation in the amputated newt forelimb.
J, Manson, R, Tassava, M, Nishikawara
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Abstract Activities of enzymes in the de novo pathway, aspartate carbamyl transferase, and salvage pathway, thymidine and uridine kinases, for nucleotide precursor synthesis were examined under conditions of innervation and denervation in the amputated newt forelimb.
J, Manson, R, Tassava, M, Nishikawara
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Dose-time effect of isoproterenol on aspartate amino-transferase and necrosis of the rat heart
Toxicology and Applied Pharmacology, 1966Abstract Single subcutaneous doses of isoproterenol (6.25, 12.5, 25, 50, and 100 mg/kg) were administered to separate groups of rats. Macroscopic lesion grades and aspartate amino-transferase activity of the hearts were determined at daily intervals until values returned to those of controls.
D G, Wenzel, R Y, Chau
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