Asymmetry of subunits of aspartate aminotransferase in solution
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چکیده
منابع مشابه
Photoinactivation of aspartate aminotransferase.
The cofactor pyridoxal 5’-phosphate bound through an aldimine linkage to lysine residues of the enzyme aspartate amiuotransferase is very stable to irradiation with light of 420 nm. The catalytic function of the enzyme exposed to light absorbed by the cofactor remains unaffected, indicating that pyridoxal 5’-phosphate is not an efficient active site photosensitizer for this aminotransferase. Th...
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1. Acetylation of aspartate aminotransferase from pig heart inhibits completely the enzymic activity when the coenzyme is in the amino form (pyridoxamine phosphate) or when the coenzyme has been removed, but not when the coenzyme is in the aldehyde form (pyridoxal phosphate). 2. The group the acylation of which is responsible for the inhibition has been identified with the in-amino group of a l...
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Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...
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The activity of aspartate aminotransferase (AST) in human serum has been widely determined as a diagnostic aid in liver disease. In this study, the effect of aluminium on AST isoenzymes in relation to aluminium intoxified patients has been investigated. Using gel filtration chromatography technique with Sephacryl S-300, mitochondrial aminotransferase (m-AST) and cytosolic aminotransferase (c-AS...
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Elevated enzyme activities in plasma may at times be attributed to the presence of macro-enzymes. The macro-enzymes are often serum enzymes in complex with immunoglobulins, resulting in a greater molecular mass that cannot be filtered by renal glomeruli and are, hence, retained in the plasma. The aspartate aminotransferase (AST) can exist as a macro-enzyme, although it has been rarely reported....
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 1987
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.000209