Inhibition of α-amylase purified from Octopus vulgaris Lam. by albumin inhibitors from wheat flour.

Octopus α-amylase has been purified to homogeneity by single-step affinity chromatography on Sepharose-bound wheat albumin inhibitors. Two electrophoretically distinguishable isoamylases are obtained, both consisting of a single polypeptide chain with molecular weight 45,000. Octopus α-amylase is more effectively inhibited by a monomeric than by a dimeric protein inhibitor from wheat. The inhibition is dependent on pH, temperature, and time of preincubation. Properties are compared with those of other animal α-amylases. [ABSTRACT FROM AUTHOR]