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[Improved procedure for purification of aspartate transaminase from chicken heart cytosol. Characterization of the enzyme].

The purification procedure reported includes fractionation of water extract from chicken hearts with ammonium sulfate, fractional precipitation with ethanol, chromatography on Whatman CM-52 cellulose and crystallization. Specific activity of the pure crystalline enzyme was 234 micromoles.min-1.mg-1, as determined in the coupled assay with malate dehydrogenase (pH 7.5; 25 degrees). The amino acid composition of the enzyme was determined and the circular dichroism spectrum was recorded in the 200-250 nm range. The spectrum shows two negative bands with extrema at 208 and 220 nm. From the circular dichroism data it is estimated that aspartate transaminase contains approximately 40% alpha-helix and 10% beta-structure.