Amino Acid Sequences of Kunitz-type Protease Inhibitors from the Sea Anemone <i>Actinia equina</i>
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- Ishida Masami
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Minagawa Sonomi
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Miyauchi Koji
- Department of Food Science and Technology, Tokyo University of Fisheries Faculty of Bioresources Sciences, Department of Marine Sciences and Resources, Nihon University
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- Shimakura Kuniyoshi
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Nagashima Yuji
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Shiomi Kazuo
- Department of Food Science and Technology, Tokyo University of Fisheries
Bibliographic Information
- Other Title
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- Amino Acid Sequences of Kunitz-type Protease Inhibitors from the Sea Anemone Actinia equina
- Amino Acid Sequences of Kunitz-type Pro
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Abstract
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.
Journal
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- Fisheries science
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Fisheries science 63 (5), 794-798, 1997
The Japanese Society of Fisheries Science
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Details 詳細情報について
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- CRID
- 1390001204430296192
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- NII Article ID
- 130003903108
- 10004871688
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- NII Book ID
- AA10993718
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- NDL BIB ID
- 4326635
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- ISSN
- 09199268
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed