| Budget Amount *help |
¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1986: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1985: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Research Abstract |
Isolation and analysis of poly rI:rC receptor on cell membrane participating in interferon induction were performed, and the following results were obtained.
1. Poly rI:rC receptor is not identical to poly rA:rU receptor, i.e. poly rI:rC receptor has the specificity to polyribonucleotide.
2. Poly rI:rC receptor is partially purified from RK-13 cell membrane by using affinity-chromatography with poly rI:rC-agarose and Fast-protein-liquid-chromatography.
3. Partially purified receptor fraction is consisted with five polypeptide with molecular weight of 95k, 80k, 66k, 59k, and 25k, respectively. By using the monoclonal antibodies to the components occuring on the surface of RK-13 cells, Western-blotting analysis was carried out, and it is suggested that the 59k-polypeptide may bear the binding site of poly rI:rC.
4. It is found that there are monoclonal antibodies to RK-13 cell surface components which enhance the interferon inducibility of poly rI:rC in RK-13 cells, as well as there are monoclonal antibodies which inhibit the binding of poly rI:rC to receptor to decrease the interferon inducubility of poly rI:rC. The mechanism of enhancement of interferon induction by monoclonal antibodies remains to be elucidated in relation to the structure and function of poly rI:rC receptor molecule.
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