1987 Fiscal Year Final Research Report Summary
Structural analysis of active site on neutral glycolipid synthase
| Project/Area Number |
61570116
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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 |
General medical chemistry
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| Research Institution | Osaka University |
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Principal Investigator |
TANIGUCHI Naovuki Professor of Biochemistry, 医学部, 教授 (90002188)
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| Project Period (FY) |
1986 – 1987
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| Keywords | Dialdehyde / Affinity label / Large subunit / 大サブユニット |
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| Research Abstract |
The dialdehyde produced by the periodate cleacage of the ribose moiety of uridine 5'-diphosphate(UDP has been used as an affinity label for the UDP-galactose/UDP binding site of <alpha>-galactosyl transferase from rat liver. This derivative causes progressive inactivation of galactosyl transferase at a rate dependent on its concentration. The substrate UDP-galactose protects the enzyme inactivation. [^3H]-UDP derivative was found to be incorporated into large subunit of the galactosyl transferase.
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