Analysis of the Molecular Structure of <I>StrePtomyces chromofuscus</I>-derived Phospholipase D

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  • SATO Hiroaki
    Department of Food Science, Faculty of Bioindustry, Tokyo University of Agriculture
  • YOSHIKANE Eriko
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • WATANABE Toshihiro
    Department of Food Science, Faculty of Bioindustry, Tokyo University of Agriculture
  • TAKANO Katsumi
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • NAGASHIMA Toshio
    Department of Food Science, Faculty of Bioindustry, Tokyo University of Agriculture
  • KOZIMA T. Tsuneo
    Department of Food Science, Faculty of Bioindustry, Tokyo University of Agriculture

Bibliographic Information

Other Title
  • <I>Streptomyces chromofuscus</I>起源Phospholipase Dの分子構造の解析
  • Analysis of the Molecular Structure of
  • Transphosphatidylational Capacity of Phospholipase D (Part I)
  • Phospholipase Dのホスファチジル基転移能に関する研究 (第1報)

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Description

When we separated the purified specimen of Streptomyces chromofuscus phospholipase D (PLase D) by SDS-PAGE, two protein bands were observed. Molecular weights of these proteins were determined to be approximately 57 and 40 kDa, respectively. As a result of N-terminal amino acid sequence analysis of these two proteins, up to 20 residues from the N-terminal amino acid were completely identical. Therefore, to evaluate the intermolecular structure of the 57 kDa protein, we performed limited proteolysis of this protein with Staphylococcus aureus V8 protease. Furthermore, regarding peptide fragments obtained as main products of limited proteolysis of the 57 kDa protein, N-terminal amino acid sequence analysis was performed. As a result, the amino acid sequence of all eight peptide fragments with molecular weights of 10, 14, 16, 18, 20, 30, 42 and 46 kDa, which were obtained by limited proteolysis of the 57 kDa protein, were found in the amino acid sequence of Streptomyces chromofuscus PLase D obtained from DNA analysis. Based on these results, it was suggested that the amino acid sequence of the 57 kDa protein was identical to that of Streptomyces chromofuscus PLase D obtained from DNA analysis.

Journal

  • Food Preservation Science

    Food Preservation Science 24 (5), 309-314, 1998

    Japan Association of Food Preservation Scientists

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