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[Spontaneous deamidation of gamma-globulin]
Voprosy Meditsinskoi Khimii
|March 1, 1978
Summary
gamma-Globulin undergoes spontaneous deamidation during incubation, altering its charge and mobility. This deamidation increases susceptibility to enzymatic attack, suggesting a role in protein aging.
Area of Science:
- Biochemistry
- Protein Chemistry
Context:
- Human blood serum gamma-globulin was studied under controlled incubation conditions.
- Protein deamidation and its effects were investigated over extended periods.
Purpose:
- To investigate the spontaneous deamidation of gamma-globulin.
- To assess the impact of deamidation on protein properties and enzymatic susceptibility.
Summary:
- Gamma-globulin was incubated at 37°C for up to 72 days.
- Changes in amide groups, amino acid content, and electrophoretic mobility were measured.
- Deamidation increased negative charge and altered mobility, enhancing susceptibility to prothelin.
Impact:
- Spontaneous deamidation contributes to changes in gamma-globulin's properties.
- This process may be a contributing factor to protein molecule aging.
- Findings provide insights into protein stability and degradation mechanisms.