Rapid Degradation of the Silkworm Diapause Hormone by Trypsin and Its Suppression by VAP-map, a Synthetic Analog of the Cuticular Peptide of Silkworm, Bm ACP-6.7(VAP-Peptide).
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- BABA Hitoshi
- Faculty of Bio-resources, Mie University
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- KATSUZAKI Hirotaka
- Faculty of Bio-resources, Mie University
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- KOMIYA Takashi
- Faculty of Bio-resources, Mie University
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- YAMASHITA Okitsugu
- Graduate School of Bioagricultural Sciences, Nagoya University
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- IMAI Kunio
- Faculty of Bio-resources, Mie University
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Abstract
Very fast tryptic degradation of the silkworm diapause hormone was found and the degradation pathway was analyzed by moderating the reaction conditions. It proceeded via cleavage at Arg23 and finally at Arg15 of DH. As the C-terminal structure of DH was essential for exhibiting bioactivity, the first cleavage caused rapid inactivation of the hormone. This tryptic digestion was strongly suppressed by adding VAP-map, a synthetic analog of the cuticular peptide of silkmoths, Bm ACP-6.7 (VAP-peptide), which is a natural synergist of DH. VAP-map suppressed the enzymic reaction by interacting with the substrate, but not with the enzyme.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 65 (5), 1033-1037, 2001
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681452938112
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- NII Article ID
- 110002680390
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD3MXktFais70%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 5782499
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- PubMed
- 11440114
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed