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In a typical papain enzymatic assay, papain was first activated by 50 mM sodium phosphate buffer (pH 7.0, 0.3 mM cysteine, 1 mM EDTA) and then was passed through Sephadex G-10 column, eluted with 50 mM sodium phosphate buffer (pH 7.0, 1 mM EDTA). The enzyme obtained in this way excluded any unexpected effect of cysteine which was necessary for initial activation. Nitrosamines were prepared in 50 mM sodium phosphate buffer (pH 7.0, 20% acetonitrile, 1 mM EDTA). Papain activity was measured spectrophotometrically at 410 nm with either UV/Visible spectrophotometer (SHIMADZU) or Spectronic Genesys 2 (Milton Roy) using chromogenic substrate N-Cbz-Glycine p-nitrophenyl ester (25 mM, 10 μL), in 1mL of 50 mM sodium phosphate buffer (pH 7.0, 1mM EDTA, 7% (v/v)acetonitrile).
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