Hydrolysis of p-nitrophenyl esters by histidine-containing linear and cyclic peptides.
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Hydrolysis of <I>p</I>-nitrophenyl acetate (PNPA) and <I>p</I>-nitrophenyl hexanoate (PNPH) catalyzed by several linear and cyclic peptides containing histidine and other amino acid residues was studied. The catalytic activity of the peptides was less than that of imidazole for PNPA and PNPH. On the other hand, in the presence of a cationic surfactant and a hydrophobic peptide the hydrolysis of PNPH was significantly enhanced.
- 公益社団法人 日本化学会の論文
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