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IMMUNOCHEMICAL PROPERTIES OF NATIVE AND DENATURED HORSE SERUM GLOBULINS.
1Department of Biochemistry, Duke University School of Medicine, Durham.
The Journal of General Physiology
|October 30, 2009
Summary
Guanidine hydrochloride causes denaturation and regeneration of antibody globulin, affecting its molecular weight and active sites. Native and denatured antibodies show similar antigenicity, suggesting close structural relationships.
Area of Science:
- Immunology
- Biochemistry
- Protein Chemistry
Background:
- Antibody globulins are crucial for immune responses.
- Understanding protein denaturation and regeneration is vital for biological studies.
- Type I antipneumococcal horse serum globulin serves as a model system.
Purpose of the Study:
- To investigate the effects of guanidine hydrochloride on antibody globulin denaturation and regeneration.
- To analyze the impact of sodium thiocyanate (NaCNS) on antibody globulin.
- To compare the antigenic properties of native, denatured, and regenerated antibody fractions.
Main Methods:
- Viscosity measurements
- Diffusion analysis
- Ultracentrifugation (sedimentation)
- Quantitative precipitin titrations
Main Results:
- Both irreversibly denatured and regenerated antibody globulin fractions were precipitable.
- Changes in combining ratios were attributed to molecular weight alterations or changes in serologically active groups.
- Native and irreversibly denatured antibody fractions exhibited similar precipitation extents.
- No significant differences in antigenic activity were found between native and irreversibly denatured fractions.
Conclusions:
- Denaturation and regeneration alter antibody globulin structure, potentially affecting molecular weight and active sites.
- Antibody globulin fractions (native and denatured) are antigenically similar.
- These findings contribute to understanding protein structure-function relationships in immunology.
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