AFFINITY CHROMATOGRAPHY OF RABBIT GASTROCNEMIUS ALPHA-L-FUCOSIDASE
Abstract
Abstract: Ct-L-Fucosidase was purified from rabbit gastrocnemius muscle usingagarose-e-aminocaproyl-fucosamine. The isolated enzyme was found to be pure by a
number of different analytical techniques including gel electrophoresis. The purified
enzyme was found essentially free of other glycosidases. The main characteristics of
the purified α-L-Fucosidase were determined; pH 6.0-6. 3, KmO.52, Vmax 25.13 n
mol/gm protein/min., Ki 0.46. L-fucosq was the only physiological competitive
inhibitor 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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