1986 Fiscal Year Final Research Report Summary
Studies on the Molecular Structure and Function of Human Monoclonal Cryoimmunoglobulins.
| Project/Area Number |
59570223
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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 |
Immunology
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| Research Institution | School of Medicine, University of Occupational and Environmental Health, Japan |
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Principal Investigator |
NAKAMURA Hiroshi Dept. of Immunol., Schl of Med., Univ. of OEH., Professor, 医学部, 教授 (60012720)
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| Co-Investigator(Kenkyū-buntansha) |
SUGIURA Tsutomu Dept. of Immunol., Schl. of Med., Univ. of OEH., Assistant, 医学部, 助手 (40131924)
NISHIMURA Yoshihisa Dept. of Immunol., Schl of Med., Univ. of OEH., Associate Professor, 医学部, 助教授 (90092288)
YAMASHITA Uki Dept. of Immunol., Schl. of Med., Univ. of OEH., Associate Professor, 医学部, 助教授 (00028680)
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| Project Period (FY) |
1984 – 1986
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| Keywords | Human monoclonal cryoglobulins / IgG3 and IgM / Cryoprecipitability / IgG3 / IgM |
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| Research Abstract |
Cryoglobulin are variety of immunoglobulins which form precipitates or gels at temperatures below 37゜ C, and are usually found in plasma of patients having chronic infectious diseases and various lymphoproliferative disorders. The clinical features are recognized by vasoconstriction of skin capillaries triggered by deposition of immunoglobulin and also by increasing viscosity of serum caused by aggregation of immunoglobulin at low temperatures. The reason for the decreased solubility of monoclonal type of cryoglobulins is not yet understood, but it appears to reflect the structure of a small and restricted part of the molecules, because of no significant difference in the primary structures between cryoglobulins and myeloma proteins belonged to the same class or subclass. In this study, the immunochemical and physico-chemical characteristics of cryoglobulins were presented by comparison with that of the myeloma proteins as control proteins, and the results were summarized as follows; 1
… More
. the specific association between homologous cryglobulin molecules, that is, no cryo-coprecipitation between cryoglobulins belonged to the same class or subclass from different patients. 2. the molecular rigidity of cryoglobulin in solution characterized by gelfiltration and viscosity measurements, and by fluorescence polarization measurements using DNS-conjugated proteins. 3. the involvement of hydrophobic amino acid residues in cryoprecipitation. 4. the characteristic CD spectra for cryoglobulins associated with the temperature-dependency. In addition, the results were obtained that the cryoprecipitate formation was susceptively inhibited by niacinamide at concentrations higher than 0.2M, and also the similar effect on antibody-antigen precipitate formation was observed by the reagent and the derivertives, suggesting that the inter-molecular interaction between hydrophobic residues might be involved in the association of cryoglobulins and the development of antibody-antigen complexes. Less
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Research Products
(12 results)
