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Abstract
An α-amylase inhibitor, Paim, obtained from the culture filtrate of Streptomyces corchorushii inhibited mammalian α-amylases except for human and rabbit, that is, Paim distinguished clearly between pig and human α-amylases, even though enzymatic properties of two amylases were very similar. EI complex formation between pig pancreatic amylase and Paim was demonstrated by gel filtration and UV difference spectroscopy. Time required for complex formation was only 60 sec. Stoichiometry between I and E was 2:1. Paim combined with human salivary amylase in a ratio of 2:1, even though Paim had no inhibitory activity against human amylase.