Abstract
The enzymatic properties of the three types of microsomal acyl-CoA desaturases, Δ 6-, Δ 9- and Δ 5-desaturases, were immunologically compared using a monospecific antibody raised against the purified linoleoyl-CoA desaturase (Δ 6-desaturase). By the double immunodiffusion technique, the anti-Δ 6-desaturase antibody showed a single precipitin line to the purified Δ 6-desaturase and microsomes treated with Triton X-100, but no line was observed with the partially purified Δ 9-desaturase. The antibody even inhibited definitely Δ 6-desaturase activity in microsomes, but neither stearoyl-CoA (Δ 9-) nor eicosatrienoic acid (Δ 5-) desaturations were inhibited. By these immunological investigations it was confirmed that terminal Δ 6-desaturase is different enzyme from desaturases Δ 9- and Δ 5.
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