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The amino acid sequence of a lambda light chain presenting abnormal physicochemical and antigenic features
European Journal of Biochemistry
|July 15, 1985
Summary
This study characterized a human monoclonal IgA1 light chain (Mem), revealing abnormal physical and antigenic properties. These abnormalities, likely conformational, were reversed by urea treatment, suggesting structural rather than sequence-based issues.
Area of Science:
- Immunology
- Molecular Biology
- Protein Chemistry
Background:
- Human monoclonal IgA1 (Mem) light chain sequence analysis.
- Characterization of V lambda I subgroup and Mcg+, Kern+, Oz- isotypes.
Purpose of the Study:
- To establish the amino acid sequence of the human monoclonal IgA1 (Mem) light chain.
- To investigate the physical and antigenic properties of the Mem light chain.
- To determine the cause of abnormal properties in the Mem light chain.
Main Methods:
- Amino acid sequencing by homology.
- SDS/polyacrylamide gel electrophoresis.
- Gel filtration chromatography.
- Gradient ultracentrifugation.
- Antigenic reactivity testing.
- Urea treatment.
Main Results:
- The Mem light chain belongs to the V lambda I subgroup and is Mcg+, Kern+, Oz-.
- Abnormal physical properties: ~10% lower apparent molecular mass than normal light chains.
- Abnormal antigenic properties: non-reactive in native state.
- Urea treatment reverted abnormalities, indicating conformational basis.
Conclusions:
- The primary amino acid sequence of the Mem light chain is normal.
- Abnormal physical and antigenic properties are due to conformational alterations.
- Conformational instability affects the Mem light chain's behavior.