osidase fromRadish (Raphanus sativus 1.)Seeds

Ana-L-arabinofuranosidase hasbeenpurified 1043-fold from radish (Raphanus sativus L.)seeds. Thepurified enzymewasa homogeneous glycoprotein consisting ofasingle polypeptide with anapparent molecular weight of64,000 andanisoelectric point value of4.7, asevidenced bydenaturing gelelectrophoresis and reversed-phase orsize-exclusion high-performance liquid chromatography andisoelectric focusing. Theenzyme characteristically catalyzes thehydrolysis ofp-nitrophenyl a-L-arabinofuranoside andp-nitrophenyl ,-D-xylopyranoside