Several properties of the partially purtially purified proteinase inhibitor in eggplant exocarp

DOI Web Site PubMed
  • 金森 正雄
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural Univerity
  • 伊吹 文男
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural Univerity
  • 山田 正明
    Research Laboratories, The Green Cross Corp.
  • 田代 操
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural Univerity
  • 三好 正満
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto Prefectural Univerity

書誌事項

タイトル別名
  • Several properties of the partially purified proteinase inhibitor in eggplant exocarp.
  • Several properties of the partially pur

この論文をさがす

説明

A proteinase inhibitor was isolated and partially purified from the exocarp of eggplant, Solanum melongena L., by means of acetate buffer extraction, heat treatment, salting-out and column chromatography on DEAF-cellulose. This preparation showed inhibitory activities on various proteinases; trypsin [EC 3. 4. 4, 4] and Pronase were strongly inhibited while α-chymotrypsin [EC 3. 4. 4. 5] and Nagarse were weakly inhibited. The inhibitor was a protein substance, and, therefore, it was gradually inactivated by the long-time incubation with Pronase. The inhibition mode was non-competitive on trypsin and competitive on Pronase on the basis of Lineweaver-Burk plots. The investigations on the inhibition behavior in the co-existence of two kinds of proteinases suggested that the inhibitor was not of multi-headed type.

収録刊行物

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