オオニシ ジュンジ onishi junji
大西 淳之
- 所属 東京家政大学 栄養学部 管理栄養学科
- 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 | Follicular fluid from human ovaries contains plasma kallikerin in free and in complex with α2-macroglobulin. |
掲載誌名 | 正式名:Biomedical Research (Tokyo, Japan) 略 称:Biomed Res ISSNコード:03886107/1880313x |
掲載区分 | 国内 |
巻・号・頁 | 18(2),pp.161-170 |
著者・共著者 | ◎Ohnishi J, Murata M, Kohyama K, Yoshida H, Wada S-I, Makinoda S, Fujimoto S, Takahashi T |
担当区分 | 筆頭著者 |
発行年月 | 1997 |
概要 | Follicular fluid from human ovaries obtained in in vitro fertilization procedures contained
substantial proteinase activities toward synthetic, arginine-containing endopeptidase substrates. Using Pro-Phe-Arg-4-methylcoumary1-7-amide as a marker for activity, two enzymes, designated human fluid serine proteinase-1 (hFSP-1) and -2 (hFSP-2), were isolated. The molecular weights of intact hFSP-1 and hFSP-2 were estimated to be approximately 90,000 and 730,000, respectively. They exhibited virtually identical substrate specificities and inhibition profiles when tested for substrates and inhibitors with low molecular weight. Polypeptide proteinase inhibitors, such as soybean trypsin inhibitor and aprotinin, strongly inhibited hFSP-1, but only inhibited hFSP-2 to a limited extent. These results, together with those of electrophoretic and immunological characterization, revealed that hFSP-1 and hFSP-2 are free plasma kallikrein and the enzyme in complex with the plasma inhibitor 0:2-macroglobulin, respectively. hFSP-1 activated human single-chain precursor tissue-type plasminogen activator. This study also indicates that the plasma kallikrein present in follicular fluid probably comes from the liver. |
DOI | doi: http://doi.org/10.2220/biomedres.18.161 |