Comparison of Phytolacain G, a Cysteine Protease from Fruit of<i>Phytolacca americana</i>, with Phytolacain R

DOI Web Site Web Site PubMed 参考文献15件 オープンアクセス

書誌事項

タイトル別名
  • Comparison of Phytolacain G, a Cysteine Protease from Fruit of Phytolacca americana, with Phytolacain R.
公開日
1998
資源種別
journal article
DOI
  • 10.1271/bbb.62.2058
公開者
公益社団法人 日本農芸化学会

この論文をさがす

説明

The enzymatic properties of phytolacain G, a protease isolated from green fruit of pokeweed, were compared with those of phytolacain R, a protease obtained from ripe fruit. The optimum pH of phytolacain G was 7.5-8.0 at 37°C using casein as the substrate. The enzyme was strongly inhibited by iodoacetic acid and p-chloromercuribenzoic acid, but not by diisopropyl fluorophosphate or EDTA. These results indicated that phytolacain G was a cysteine protease, like phytolacain R. Nine sites of oxidized insulin B-chain were cleaved by phytolacain G during 20 h of hydrolysis. The six sites cleaved by phytolacain G were also cleaved by phytolacain R. The substrate specificity of phytolacain G was broad, but the preference for hydrophobic residues at the P2 position was similar to the substrate specificity of papain. The amino-terminal sequence of phytolacain G was not identical with that of phytolacain R; however, the amino acid residues conserved in the papain family were also conserved in this enzyme.<br>

収録刊行物

参考文献 (15)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ