| Abstrakt: |
The number of arginine residues of pigeon breast muscle alpha-ketoglutarate dehydrogenase modified by 2,3-butanedione and 2,4-pentanedione was determined. It was shown that two of the 40 arginine residues in the enzyme monomer (Mr = 86,000) are accessible to the action of dicarbonyl compounds and are functionally significant. The protective effect of alpha-ketoglutarate and ADP against enzyme modification by 2,3-butanedione suggests the participation of alpha-ketoglutarate dehydrogenase arginine residues in the binding of substrate and allosteric activator, ADP. |
