AFFINITY CHROMATOGRAPHY OF RABBIT GASTROCNEMIUS ALPHA-L-FUCOSIDASE

Authors

  • J.A. Khan
  • M.H.R. Lewis

Abstract

Abstract: Ct-L-Fucosidase was purified from rabbit gastrocnemius muscle usingagarose-e-aminocaproyl-fucosamine. The isolated enzyme was found to be pure by anumber of different analytical techniques including gel electrophoresis. The purifiedenzyme was found essentially free of other glycosidases. The main characteristics ofthe purified α-L-Fucosidase were determined; pH 6.0-6. 3, KmO.52, Vmax 25.13 nmol/gm protein/min., Ki 0.46. L-fucosq was the only physiological competitiveinhibitor of the enzyme. Ct-L-fucosidase is heat labile and stable for 2-3 months at —20 C in the presence of lOOmM L-fucose. The purified enzyme showed 50,000 Mol.Wt. on SDS-Electrophoresis.

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