title: Purification and characterization of ovine pancreatic alpha - amylase.
abstract: Ovine pancreatic amylase has been purified from pancreas homogenate by ammonium sulfate, acetone precipitation, DEAE-cellulose chromatography and finally by specific adsorption on polydextran gel. The enzyme is homogeneous and found as a single form as shown by disc electrophoresis, SDS gel electrophoresis, electrofocusing and ultracentrifugation. Its specific activity is similar to that of porcine amylase. The amino acid composition indicates a high content in aromatic and acidic amino acids as for the porcine enzyme; however the methionine and half cystine content differ widely. The N-terminal end is blocked. Also ovine amylase is glycosylated. The molecular weight (56,000-58,000) is slightly higher than for the porcine enzyme. The isoelectric point is acidic (pI = 3.2).
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000681:Amylases / Q000302:isolation & purification*; D000818:Animals; D007526:Isoelectric Point; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D012756:Sheep
chemical_list: D000596:Amino Acids; D000681:Amylases