Purification and Characterization of Phospholipase D from Cabbage Leaves.

• SATO Hiroaki

  Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture

• WATANABE Toshihiro

  Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture

• SAGANE Yoshimasa

  Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture

• NAKAZAWA Yozo

  Department of Applied Biology and Chemistry, Faculty of Applied Bio-Science, Tokyo University of Agriculture

• TAKANO Katsumi

  Department of Applied Biology and Chemistry, Faculty of Applied Bio-Science, Tokyo University of Agriculture

抄録

Phospholipase D (PLD) was purified from cabbage leaves. The molecular weight of purified PLD was estimated as approximately 73 and 87 kDa by gel filtration using Superdex 200 HR column and, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), respectively. The transphosphatidylation capacity for phosphatidylcholine of this enzyme reached over 90% , and the enzyme's hydrolysis efficiency for phosphatidylcholine was five-fold higher than that for phosphatidylglycerol. These findings indicated that the cabbage PLD efficiently transferred phosphatidylcholine to phosphatidylglycerol. On N-terminal amino acid sequence analysis of the band separated by SDSPAGE, two sequences with differing N-terminus were detected. This N-terminal difference may have been generated by processing during maturation of PLD.

収録刊行物

• Food Science and Technology Research

  Food Science and Technology Research 6 (1), 29-33, 2000

  公益社団法人 日本食品科学工学会

キーワード

• phospholipase D
• cabbage
• N-terminal amino acid sequence

詳細情報

• CRID: 1390282679431200640
• NII論文ID: 10013007762
• NII書誌ID: AA11320122
• DOI: 10.3136/fstr.6.29
• ISSN: 18813984
• ISSN: 13446606
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可