オオニシ ジュンジ  onishi junji
大西 淳之

  • 所属   東京家政大学  家政学部 栄養学科
  •     東京家政大学大学院  人間生活学総合研究科 健康栄養学専攻
  •     東京家政大学大学院  人間生活学総合研究科 人間生活学専攻
  •     東京家政大学短期大学部  短期大学部 栄養科
  • 職種   教授
論文種別 原著
言語種別 英語
査読の有無 査読あり
表題 Identification and partial characterization of a metallpeptidase from porcine ovaries.
掲載誌名 正式名:Journal of experimental zoology. Part A, Comparative experimental biology
略  称:J Exp Zoolog A Comp Exp Biol
ISSNコード:15488969/1552499X
掲載区分国外
巻・号・頁 281(6),pp.574-581
著者・共著者 ◎Takahashi T, Matsui H, Kihara T, Kimura A, Ohnishi J.
担当区分 最終著者
発行年月 1998/08
概要 The follicular fluid of porcine ovaries contains an EDTA-sensitive enzyme activity for the synthetic substrate benzyloxycarbonyl-Val-Lys-Met-4-methylcoumaryl-7-amide. To investigate its characteristics and its identification, the enzyme was partially purified by ammonium sulfate fractionation followed by column chromatographies on DEAE-Cellulose and chelating Cellulofine columns. The enzyme activity was strongly inhibited by typical chelators, such as EDTA and o-phenanthroline, but after inhibition by EDTA the activity was completely restored with an appropriate amount of Zn2+ and Co2+ ions. It showed enzyme activity solely for benzyloxycarbonyl-Val-Lys-Met-4-methylcoumaryl-7-amide among the substrates tested. The molecular weight of the enzyme was estimated to be 400,000 by gel filtration. The enzyme activity in the fluid obtained from large follicles of porcine ovaries was significantly higher than that from smaller follicles. It appeared that the granulosa cell extract did not contain the metalloenzyme activity. Similar enzyme activities were detected in follicular fluids from bovine and human ovaries. These results suggest that the present enzyme is distinct from any other metalloendopeptidases thus far reported.