[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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001219:Aspartate Aminotransferases / Q000302:isolation & purification* / Q000378:metabolism; D002645:Chickens; D002942:Circular Dichroism; D003460:Crystallization; D003600:Cytosol / Q000201:enzymology; D008722:Methods; D009206:Myocardium / Q000201:enzymology*; D011487:Protein Conformation
D000596:Amino Acids; D001219:Aspartate Aminotransferases
Uluchshennyĭ metod ochistki aspartat-transaminazy iz tsitozolia kurinykh serdets i kharakteristika preparatov fermenta.