Amino Acid Sequences of Kunitz-type Protease Inhibitors from the Sea Anemone Actinia equina

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  • Ishida Masami
    Department of Food Science and Technology, Tokyo University of Fisheries
  • Minagawa Sonomi
    Department of Food Science and Technology, Tokyo University of Fisheries
  • Miyauchi Koji
    Department of Food Science and Technology, Tokyo University of Fisheries Faculty of Bioresources Sciences, Department of Marine Sciences and Resources, Nihon University
  • Shimakura Kuniyoshi
    Department of Food Science and Technology, Tokyo University of Fisheries
  • Nagashima Yuji
    Department of Food Science and Technology, Tokyo University of Fisheries
  • Shiomi Kazuo
    Department of Food Science and Technology, Tokyo University of Fisheries

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タイトル別名
  • Amino Acid Sequences of Kunitz-type Protease Inhibitors from the Sea Anemone <i>Actinia equina</i>
  • Amino Acid Sequences of Kunitz-type Pro

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抄録

Four serine protease inhibitors (AEPI-I, II, III and IV) were isolated from the sea anemone Actinia equina by a slight modification of our previous method. When the native inhibitors were applied to a sequencer, 36, 36, 35, and 37 amino acid residues from the N-terminus were identified for AEPI-I, II, III, and IV, respectively. The remaining sequences of AEPI-I and II were deduced from analyses of peptide fragments obtained by digestion of S-carboxamidomethylated molecules with either V8 protease or lysyl endopeptidase. Both inhibitors were composed of 59 amino acid residues including 6 half-Cys residues and their sequences were very similar to each other with replacements at only two positions. The positions of half-Cys residues and the entire-chain homology identified these inhibitors as members of the Kunitz-type family. Notably, the sequences of the two contact sites with serine proteases were highly conserved within the sea anemone inhibitors.

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