Purification and Characterization of Rice Embryo BAPAase (Benzoyl-L-arginine p-nitroanilide Hydrolase)

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Benzoyl-L-arginine p-nitroanilide hydrolase (BAPAase), which has both endopeptidase and carboxypeptidase activity toward the Arg-X or Lys-X bond of small peptides [Shibata and Doi (1984) Plant 〓 Cell Physiol. 25:1421], was purified from rice embryos by ammonium sulfate and polymin fractionations and by ion exchange, gel exclusion and hydrophobic chromatographies. The purified enzyme was homogeneous when analyzed by polyacrylamide gel electrophoresis. It was unstable in the absence of surface-active reagents such as Triton X-100. Maximum activity for benzoyl-L-arginine p-nitroanilide (L-BAPA) or carboxypeptidase activity toward butoxycarbonyl-Gly-Lys-Leu was obtained at pH 9.0. L-BAPA at high concentrations inhibited the enzyme's activity. Di-isopropyl phosphofluoridate, N-tosyl-L-Iysine chloromethyl ketone, leupeptin and anti pain, which are specific inhibitors of trypsin, inhibited BAPAase activity, but soybean and rice bran trypsin inhibitor had no effect on it. Sulfhydryl reagents strongly inhibited the BAPAase activity.
日本植物生理学会の論文