1988 Fiscal Year Final Research Report Summary
Analysis of the molecular mechanism of pepsinogen activation with techniques of protein chemistry
| Project/Area Number |
62580119
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Primate Research Institute, Kyoto University |
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Principal Investigator |
KAGEYAMA Takashi Primate Research Institute, Kyoto University, 霊長類研究所, 助教授 (20027501)
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| Co-Investigator(Kenkyū-buntansha) |
ASAOKA Kazuo Primate Research Institute, Kyoto University, 霊長類研究所, 教務職員 (10089138)
HAYASHI Motoharu Primate Research Institute, Kyoto University, 霊長類研究所, 助手 (10027500)
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| Project Period (FY) |
1987 – 1988
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| Keywords | Pepsinogen / Pepsin / ペプシノーゲンの活性化 |
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| Research Abstract |
Pepsinogen is activated to pepsin by releasing its NH2-terminal 44-47 residues. Two highly susceptible sites of cleavage are present in the activation segments. One site is the bond between the activation segment and the pepsin moiety (P-site) and the other is a bond located in the central region of the activation segment (I-site). When the P-site is cleaved first, pepsinnogen is converted to pepsin directly with the release of the intact activation segment. On the other hand, when the I-site is cleaved first, an intermediate form is generated,. In this case, further cleavages are necessary to complete the activation and therefore the activation is essentially a stepwise process. Both intramolecular and intermolecular reactions are involved in these cleavages. The intramolecular clevage of the P-site or the I-site is important as an initiating reaction to generate active molecules. However, the intermolecular cleavage of the P-site is essential to accelerate and complete the activation.
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