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. 1966 Jun;99(3):589-94.
doi: 10.1042/bj0990589.

Purification and general properties of aspartate aminotransferase of ox heart

G Marino, A M Greco, V Scardi, R Zito

Purification and general properties of aspartate aminotransferase of ox heart

G Marino et al. Biochem J. 1966 Jun.

Abstract

1. A five-step procedure for preparing highly purified aspartate aminotransferase from ox heart is described. 2. The homogeneity of the pure enzyme was established by criteria such as ultracentrifugation and electrophoresis in starch gel and in polyacrylamide gel. 3. The pure enzyme has an isoelectric point of about pH5, and E(1%) (1cm.) 14.40 at 278mmu. 4. The molecular weight of the pure enzyme was determined as 96000 by sedimentation equilibrium. 5. The pH optimum for the pure enzyme was about 8. It was determined by a new assay technique. 6. A difference in the electrophoretic migration rate between the enzyme from ox heart and brain and the enzyme from pig heart and brain suggests a species specificity rather than an organ specificity. 7. A new effect of deionization on the visible-absorption spectrum of the enzyme was observed.

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References

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