Purification and characterization of an acid proteinase from human uterine cervix.

• 伊東 晃

• 森 陽

• 平川 舜

抄録

Acid and neutral proteinases are distributed in the cervical stroma of the human uterus, and the former activity is about 10 times that of the latter. The acid proteinase was completely separated from the neutral enzyme by Sephadex G-200 gel filtration and the acid enzyme was purified about 630-fold to homogenity by ion-exchange chromato-graphy on DEAE-Sephadex A-50 and rechromatography on Sephadex G-200. The purified acid proteinase showed the optimum pH in the range from 3.4 to 3.6 for acid-and ureadenatured bovine hemoglobins, and was completely inhibited by pepstatin and N-bromosuccinimide. Its molecular weight was calculated to be 4.2×10⁴ by gel filtration on Sephadex G-75. From these results, this enzyme could be identified as cathepsin D.

収録刊行物

• ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ

  ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ 27 (4), 969-973, 1979

  公益社団法人 日本薬学会

キーワード

• cervical stroma

詳細情報

• CRID: 1390001204172355584
• NII論文ID: 110003662277
• NII書誌ID: AA00602100
• DOI: 10.1248/cpb.27.969
• ISSN: 13475223
• ISSN: 00092363
• PubMed: 476865
• Web Site: http://www.jstage.jst.go.jp/article/cpb1958/27/4/27_4_969/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/1980010250
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可