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[17] Glutamate-aspartate transaminase from microorganisms
1985Publisher Summary Various methods have been developed for the assay of aspartate aminotransferase. Most of these depend on the determination of oxalacetate or L-glutamate. Out of these, the Karmen method is used most widely, particularly in the field of clinical analysis, in which oxalacetate is determined with malate dehydrogenase and NADH by ...
Toshiharu Yagi +3 more
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MITOCHONDRIAL ASPARTATE TRANSAMINASE
The Lancet, 1970S N, Farmer, A M, Nanji, T R, Boyde
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Reversible dissociation of succinylated aspartate transaminase into subunits
Biochemical and Biophysical Research Communications, 1965Abstract The molecule of succinylated aspartate-transaminase (mol. weight 117,000) dissociates into two subunits in alkaline solutions. Upon reneutralization to pH 6.5 the enzyme subunits reassociate. In the region of pH-optimum (pH 8.5–9.3) succinylated transaminase retains 65 per cent of the catalytic activity of native transaminase.
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Circular dichroism of aspartate transaminase
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964Y N, BREUSOV +3 more
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Inhibition of Glutamic-Aspartic Transaminase by Antibodies
Nature, 1962F, CORDOBA, C, GONZALEZ, A, PEREZ
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Specificity and resolution of glutamate-aspartate transaminase
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964A, NOVOGRODSKY, A, MEISTER
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On the acetylation of glutamic aspartic transaminase
Archives of Biochemistry and Biophysics, 1962C, TURANO, A, GIARTOSIO, P, VECCHINI
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LIVER GLUTAMIC-ASPARTIC TRANSAMINASE ACTIVITY IN DIABETES
The Lancet, 1959S J, PATRICK, J A, TULLOCH
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