Abstract
The inhibition of bands 5 and 1 isoenzymes of porcine lactate dehydrogenase by salicylate was investigated kinetically. These studies indicated that up to two molecules of salicylate could combine with the active site of the free band 5 isoenzyme, and that one of the two salicylate molecules competes with its AMP binding site. It is concluded that salicylate competes with the AMP moiety of NAD+ in this enzyme.
Original language | English |
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Pages (from-to) | 637-643 |
Number of pages | 7 |
Journal | International Journal of Biochemistry |
Volume | 8 |
Issue number | 9 |
Publication status | Published - 1977 |