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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.
V M Kochkina, and
A V Azarian, and
M L Mekhanik, and
L N Zakomyrdina, and
N I Sinitsyna
January 1977,
Molekuliarnaia biologiia,
V M Kochkina, and
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January 1985,
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Biokhimiia (Moscow, Russia),
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Biokhimiia (Moscow, Russia),
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N I Sinitsyna
January 1975,
Biokhimiia (Moscow, Russia),
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M L Mekhanik, and
L N Zakomyrdina, and
N I Sinitsyna
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Biochemical and biophysical research communications,
V M Kochkina, and
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Biokhimiia (Moscow, Russia),
V M Kochkina, and
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M L Mekhanik, and
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N I Sinitsyna
January 1975,
Biokhimiia (Moscow, Russia),
V M Kochkina, and
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May 1980,
FEBS letters,
V M Kochkina, and
A V Azarian, and
M L Mekhanik, and
L N Zakomyrdina, and
N I Sinitsyna
September 1973,
FEBS letters,
