Structural and Functional Analyses of a Strong Chitin-Binding Protein-1 (SCBP-1) from the Exoskeleton of the Crayfish Procambarus clarkii
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- SUZUKI Michio
- Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo Department of Earth and Planetary Science, Graduate School of Science, The University of Tokyo
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- SUGISAKA-NOBAYASHI Arisa
- Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo
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- KOGURE Toshihiro
- Department of Earth and Planetary Science, Graduate School of Science, The University of Tokyo
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- NAGASAWA Hiromichi
- Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo
書誌事項
- タイトル別名
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- Structural and Functional Analyses of a Strong Chitin-Binding Protein-1 (SCBP-1) from the Exoskeleton of the Crayfish <i>Procambarus clarkii</i>
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The organic matrices in the exoskeleton of the crayfish Procambarus clarkii are classified into three groups depending on solubility; acid soluble, acid insoluble-SDS/dithiothreitol (DTT) soluble, and acid insoluble-SDS/DTT insoluble fractions. In our previous studies, Casp-1 and -2 were identified in the acid soluble fraction, and CAP-1 and -2 were identified in the acid insoluble-SDS/DTT soluble fraction. In this study, acid insoluble-SDS/DTT insoluble materials were digested with proteases and the resulting peptides were purified and sequenced. Based on the sequences, a cDNA encoding this protein was cloned. The whole primary sequence of the matrix protein named strong chitin-binding protein-1 (SCBP-1), was deduced. SCBP-1 consisted of 155 amino acid residues and had a Rebers-Riddiford consensus sequence for chitin binding. A recombinant protein of SCBP-N corresponding to the N-terminal part of SCBP-1 showed no chitin-binding ability, while SCBP-C corresponding to the C-terminal part of SCBP-1, showed weak affinity to chitin. These results suggest that the primary sequence of SCBP-1 does not have strong chitin-binding ability. Therefore, SCBP-1 probably binds covalently to chitin through a particular residue contained in the peptide part that was not obtained by protease digestion.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 77 (2), 361-368, 2013
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681456810880
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- NII論文ID
- 10031164741
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- NII書誌ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC3szmsFKrug%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 024295541
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- PubMed
- 23391933
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- 使用不可