Shanker, J. ; Datta, K. (1983) Purification and properties of L-alanine dioxovaleric acid transaminase from rat liver mitochondria Biochemistry International, 7 (1). pp. 23-31. ISSN 0158-5231
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Abstract
L-alanine:4,5-dioxovalerate transaminase (EC 2.6.1.44) has been purified to homogeneity from rat liver mitochondria. Molecular weight of the native enzyme is estimated to be 230,000 ± 3000 by gel filtration. Under denaturing condition, the dissociated enzyme has a subunit of approximately 41,000 ±2000, indicating the enzyme apparently is composed of six identical subunits. The enzyme is heat stable and has optimal activity at pH 6.9. Km values for L-alanine and 4,5-dioxovalerate are 3.3 × 10(-3) M and 2.8 × 10(-4) M respectively. Excess dioxovalerate inhibits the enzyme activity. Pyridoxal phosphate and dithiothreitol also inhibit the enzyme activity.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to International Union of Biochemistry. |
| ID Code: | 75127 |
| Deposited On: | 21 Dec 2011 14:14 |
| Last Modified: | 21 Dec 2011 14:14 |
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