1992 Fiscal Year Final Research Report Summary
Research for structure-function relationship in human gonadotropins
| Project/Area Number |
02454379
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Obstetrics and gynecology
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| Research Institution | Nagoya University |
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Principal Investigator |
SUGANUMA Nobuhiko Nagoya University,School of Medicine Associate Professor, 医学部, 助教授 (30179113)
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| Co-Investigator(Kenkyū-buntansha) |
SEO Hisao Nagoya University, Research Institute of Environmental Medicine,Professor, 環境医学研究所, 教授 (40135380)
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| Project Period (FY) |
1990 – 1992
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| Keywords | human chorionic gonadotropin / luteinizing hormone / follicle stimulating hormone / beta subunit / disulfide bond / site-directed mutagenesis / expression vector / gene expression |
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| Research Abstract |
To analyze the intracellular roles of disulfide bonds in human gonadotropins, the cystein residues in each beta subunit were converted to other amino acid sequences by site-directed mutagenesis. The following results were obtained using the mutant beta subunits.
1. Assembly with alpha subunit was blocked by the elimination of any disulfide bonds in hCG beta subunit, however, there were differences in the binding rate among each disulfide pair.
2. The disulfide bond at cysteins 26/110 had regulating role in secretions of beta subunits of hCG and LH,but not in FSH beta subunit.
3. Various immunological reactivities were observed when the disulfide bond at 23/72 in hCGbeta were eliminated.
4. Receptor bindings and biological activities were not affected by disulfide bond breakage in hCGbeta.
5. The process of disulfide bond formation in hCGbeta were also determined. These methods presented here could be useful to analyze the relationship between structure and function even in other peptides.
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