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Aspartate aminotransferase from the cytosolic fraction of chicken brain was isolated with acceptable yield and high degree of purity. The enzyme appeared in multiple molecular forms: alpha, beta, gamma, and delta (alpha predominates), as detected by polyacrylamide gel electrophoresis with specific staining. These different forms of the enzyme were separated by DEAE-Sephacel chromatography, and showed different isoelectric points and maximal velocities values, whereas their molecular weight, optimum pH and Michaelis constants were very similar. Generation process studies suggest that minors subforms of the enzyme could be raised from alpha form by a mechanism in which the oxidation of particular amino acid groups are involved.
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
January 1988,
Enzyme,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
January 1968,
Biochemistry,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
June 1964,
Bollettino della Societa italiana di biologia sperimentale,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
November 1978,
Biochemical and biophysical research communications,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
September 1980,
Biochemistry,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
January 1984,
Progress in clinical and biological research,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
January 1974,
The Italian journal of biochemistry,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
January 1975,
Biokhimiia (Moscow, Russia),
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
February 2002,
Journal of enzyme inhibition and medicinal chemistry,
S Imperial, and
M Busquets, and
A Cortés, and
J Bozal
April 1989,
Biochimie,
