Characterization of two endopolygalacturonase isozymes produced by Fusarium oxysporum f. sp. lycopersici Public Deposited

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  • Polygalacturonase produced by Fusarium oxysporum f. sp. lycopersici was purified by chromatography on DEAE cellulose, CM cellulose, and hydroxylapatite. Removal of large amounts of carbohydrate by chromatography on hydroxylapatite did not affect heat stability of the enzyme. A large proportion of the remaining carbohydrate appeared to be covalently linked to the enzyme protein. The purified enzyme consisted of two electrophoretically distinct "isozymes. " The two had similar "endo" modes of action on polygalacturonic acid, as determined by comparison of viscosity reduction, reducing group release, and thin layer chromatography of oligomeric hydrolysis products. Both isozymes hydrolyzed 5% of the substrate bonds in reaching 50% viscosity reduction. The amino acid compositions of the isozymes were similar and their molecular weights were about 37, 000 as determined by sedimentation equilibrium, Electrophoresis in several different concentrations of polyacrylamide gel indicated the two isozymes were charge isomers.
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