2000 Fiscal Year Final Research Report Summary
Biological significance of multivalent interaction between animal lectins and saccharides.
| Project/Area Number |
11680614
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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 |
Structural biochemistry
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| Research Institution | Teikyo University |
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Principal Investigator |
KASAI Kenichi Teikyo Univ., Fac.Pharm.Sci., Professor, 薬学部, 教授 (40001052)
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| Co-Investigator(Kenkyū-buntansha) |
HIRABAYASHI Jun Teikyo Univ., Fac.Pharm.Sci., Lecturer, 薬学部, 講師 (40156691)
SHIMURA Kenichi Teikyo Univ., Fac.Pharm.Sci., Asc.Professor, 薬学部, 助教授 (30130008)
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| Project Period (FY) |
1999 – 2000
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| Keywords | Galectin / Glycosignal / Specific interaction / Multivalent interaction / Frontal affinity chromatography / C.elegans |
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| Research Abstract |
Almost all lectins so far investigated have multiple sugar-binding sites and perform multivalent interaction with various glycoconjugates. Since the most important clue to understand the role of lectins as members of the biological regulatory machines should be hiddent in these phenomena, we planned to elucidate the principle and mechanism of multivalent interaction by using the members of the galectin family which is one of the typical animnal lectins. For the purpose of conducting such a pioneering work, it was essential to develop new powerful analytical tools. We, therefore, reinforced frontal affinity chromatography and capillary electrophoresis which we have developed as sensitive, rapid and accurate analytical tools for specific interaction between biomolecules. We applied these new tools to analyze systematically interaction between a variety of sugars and recombinant galectins prepared from vertebrates, nematode, and sponges. Sugar-binding profiles obtained for these galectins provided us with many useful data for the understanding of intra-and extracellular functions, molecular evolution, and other various aspects of galectins. Basic knowledge concerning multivalent interactions was obtained, and it was strongly suggested that association of galectin molecules on cell surface may dramatically affect the interaction with multivalent glycoconjugates.
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