Ostrich pancreatic α-amylase (OPA) was purified to homogeneity in the presence of protease inhibitors by a single-step affinity chromatography technique. The first 53 amino acids of the N-terminus were identified by gas-phase sequencing. From kinetic parameters (kcat/Km) a subsite profile was established leading to a five subsite model for OPA. The pKa values of catalytic residues were determined as 5.75 and 8.36. Inhibition of OPA by monosaccharides, β-cyclodextrin and a wheat α-amylase inhibitor was studied.
- Ostrich Pancreas α-Amylase N-terminal sequence Subsite profile
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