Abstract
Rat pancreatic and salivary amylase [(1 → 4) α- d-glucan glucanohydrolase] (EC 3.2.1.1) were purified 20- to 50-fold with a yield above 75% by a single-step affinity chromatographic procedure. The affinity ligand was an α-glucohydrolase inhibitor (proprietary name Bay g5421) coupled to ω-aminohexyl-Sepharose 4B. Pancreatic amylase was eluted as a single peak at pH 7.4 with 0.1% glycogen or at pH 5.8 without glycogen. Salivary amylase could be eluted only with 0.1% glycogen containing buffer at pH 7.4. Pancreatic amylase migrated as a single homogeneous band on sodium dodecyl sulfate polyacrylamide gels, whereas salivary amylase migrated as a doublet.
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