Purification and Properties of Aminopeptidase C from Chicken Skeletal Muscle.

• NISHIMURA Toshihide

  Department of Agricultural Chemistry, The University of Tokyo

• KATO Yutaka

  Research Institute, Soda Aromatic Co., Ltd.

• OKITANI Akihiro

  Department of Food Science, Nippon Veterinary and Animal Science University

• KATO Hiromichi

  Department of Agricultural Chemistry, The University of Tokyo

抄録

Aminopeptidase C was purified from fresh chicken skeletal muscle by ammonium sulfate fractionation, and by successive chromatography on DEAE-cellulose, Ultrogel AcA 34, DEAE-cellulose again, and an alanine AH-Sepharose 4B affinity column twice. The purified enzyme migrated as a single band by SDS-PAGE. Aminopeptidase C was purified about 300-fold over the crude extract with a yield of 0.6%. The molecular weight of this enzyme was found to be 185, 000 by gel filtration in a Sepharose 6B column and 92, 000 by SDS-PAGE. The optimum pH for the hydrolysis of L-leucine β-naphthylamide was 6.0-7.0, the enzyme being stable in the range of pH 6.5-8.0. The activity of this enzyme was strongly inhibited by EDTA and puromycin, and was high against the β-naphthylamide derivatives of Lys, Leu, Ala and Met. The enzyme was more active towards tri- and tetrapeptides than towards dipeptides.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 55 (7), 1771-1778, 1991

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681439370624
• NII論文ID: 110006325631
• NII書誌ID: AA00515312
• DOI: 10.1271/bbb1961.55.1771
• COI: 1:CAS:528:DyaK3MXlslOqs7w%3D
• ISSN: 18811280
• ISSN: 00021369
• ISSN: http://id.crossref.org/issn/00021369
• PubMed: 1368717
• 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