キノコフロテアーゼの精製と性質 : 4. マイタケ Grifola frondosa

概要

論文の詳細を見る
An endopeptidase was purified to apparent homogeneity from the fruit body of maitake mushroom, Grifola frondosa, by ammonium sulfate precipitation, gel filtration, hydrophobic chromarography and Ion-exchange chromatography using tbutyloxycarbonyl-Ala-Ala-Pro-Phe p-nitroanilide as a substrate. Studies on the substrate specificity with a series of synthetic peptide p-nitroanilides showed that the enzyme preferentially hydrolyzed peptide bond of the carboxyl-terminal side of phenylalanine with proline residue at P_2 subsite, and slowly hydrolyzed the leucine and histidine peptide bonds of P_2 proline substrates. On the other hand, peptide p-nitroanilides with leucine residue at P_2 position were not hydrolyzed by the enzyme. The enzyme was almost completely inactivated by diisopropyl phosphofluoridate. Thus, the maitake peptidase was shown to be a serine protease with chymotrypsin-like specificity.
福岡女子大学の論文
2001-01-31