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 Cleavage specificity of porcine follipsin.
掲載誌名 正式名:The Journal of Biological Chemistry
略  称:J Biol Chem
ISSNコード:00219258/1083351X
掲載区分国外
巻・号・頁 270(33),pp.19391-19394
著者・共著者 ◎Ohnishi J, Kihara T, Hamabata T, Takahashi K, Takahashi T.
発行年月 1995/08
概要 Follipsin purified from the follicular fluid of porcine ovaries was studied for its specificity against various synthetic and peptide substrates. The enzyme cleaved only by an endopeptidase activity at the amide and peptide bonds of Arg-X, indicating strict specificity of the S1 pocket for arginine. The specificity for pocket S2 appears to favor either hydrophobic or basic side chains. A 10-residue peptide containing a portion of the activation site of human tissue plasminogen activator was synthesized and tested with the enzyme. The peptide was cleaved by follipsin at the Arg-Ile bond, as expected from the specificity deduced above. Furthermore, the enzyme successfully converted single-chain precursor tissue plasminogen activator (sctPA) to its active, two-chain form by cleaving the corresponding peptide bond. Comparison of the rates of single-chain precursor tissue plasminogen activator activation and tissue plasminogen activator peptide hydrolysis revealed that the former is a more efficient substrate than the latter.
PMID PMID: 7642619