An LDH isoenzyme was purified to homogeneity from uromastix testes and its inhibition spectrum towards known LDH isoenzyme inhibitors studied. Platinum compounds inhibited the enzyme in the forward reaction (pyruvate-->lactate) only, n-hexanediol and colchicine showed no inhibition and gossypol acetic acid (GAA) strongly inhibited both the forward and reverse reactions and the reactions were time-dependent. Oxalate caused non-competitive inhibition (Ki app = IC50 = 0.15 mM) of the forward reaction, NADH was more effective in blocking inhibition by GAA than pyruvate. This enzyme was also unable to use ketocaproic acid as a substrate.