Jul 1, 1977

Human pancreatic alpha-amylase. I. Purification and characterization

Annals of Clinical and Laboratory Science
H H Sky-Peck, P Thuvasethakul

Abstract

alpha-Amylase was extracted from human pancreas and purified by using ammonium sulfate fractionation, Sephadex G-100 and DEAE-Sephadex A-50 column chromatography. The enzyme was shown to be homogenous by three different criteria: polyacrylamide disc gel electrophoresis, SDS polyacrylamide gel electrophoresis and analytical ultracentrifugation. The values of SO20,w, D20,w, v, and frictional ration of the enzyme were calculated to be 5.01S, 7.56D, 0.718 ml g-1 and 1.10, respectively. The molecular weight of the alpha-amylase was determined by three different methods: sedimentation velocity-diffusion, conventional sedimentation equilibrium and SDS polyacrylamide gel electrophoresis and was found to be 57,850; 50,100 and 53,200 g mole-1, respectively (average value 53,700). The amino acid composition of the enzyme was determined and compared with those of alpha-amylases from various other sources.

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Mentioned in this Paper

Analytical Ultracentrifugation
Nevus
Talpidae
SDS-PAGE
Benign Tumor of Pancreas
Hydatidiform Mole
DEAE-Sephadex A-50
Electrophoresis, Disc
Amylases
Purification Aspects

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