Jan 1, 1975

Purification and characterization of ovine pancreatic alpha - amylase

Biochimie
M EttalibiG Marchis-Mouren

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).

  • References9
  • Citations1

Mentioned in this Paper

Amino Acids, I.V. solution additive
Benign Tumor of Pancreas
Chromatography, DEAE-Cellulose
Dall Sheep
Acetone Measurement
Adsorption
Pancreatic amylase
Amylase Measurement
Electrophoresis, Disc
Aromatics

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