Purification and characterization of chicken brain cytosolic aspartate aminotransferase.
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.
Departament de Bioquimica i Fisiologia, Facultat de Quimica, Universitat de Barcelona, Spain.
S
S
Imperial
M
M
Busquets
A
A
Cortés
J
J
Bozal
D000818:Animals; D001219:Aspartate Aminotransferases / Q000302:isolation & purification*; D001921:Brain / Q000201:enzymology*; D002645:Chickens; D002845:Chromatography; D003600:Cytosol / Q000201:enzymology; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification; D007700:Kinetics; D008970:Molecular Weight
D007527:Isoenzymes; D001219:Aspartate Aminotransferases