| Project/Area Number |
07640900
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
動物生理・代謝
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
KAGEYAMA Takashi Kyoto University, Primate Research Institute, Associate Professor, 霊長類研究所, 助教授 (20027501)
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| Co-Investigator(Kenkyū-buntansha) |
ASAOKA Kazuo Kyoto University, Primate Research Institute, Instructor, 霊長類研究所, 助手 (10089138)
YONEZAWA Satoshi Aichi Human Service Center, Institure for Developmental Research, Leader, 発達障害研究所, 室長 (90001867)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1996: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1995: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | cathepsin E / processing / biologically active peptides / invariant chain / new assay method |
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| Research Abstract |
1.Cathepsin E processed the precursors of the neurotensin, neuromedin, xenopsin, and related bioactive peptides. The common structural features that specified the processing sites were found in the carboxyl-terminal sequences of the active peptides of these precursors ; namely, the sequence Pro-X-X'-hydrophobic amino acid was found at positions P4 through P1.
2.Cathepsin E processed invariant chain to CLIP.The sequence of the P4 through P1 of the cleavage site was Pro-Leu-Leu-Met, and this was consistent with the consensus sequence that is recognized by cathepsin E.
3.A new method for the assay of cathepsin E was developed. The method was based on the specific activity of cathepsin E against substance P.
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