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The Lewis antigens and secretor status
The Japanese Journal of Antibiotics
|December 1, 1979
Summary
This study explores the three-dimensional structures of ABH and LEWIS antigens, finding that de-acetylated LEWIS-b and LEWIS-d antigens can bind to Ulex europaeus lectin, suggesting their presence in amine form in saliva.
Area of Science:
- Carbohydrate chemistry
- Immunochemistry
- Structural biology
Background:
- ABH and LEWIS antigens are crucial in human blood groups and tissue typing.
- The interaction between these antigens and their binding sites is not fully understood at a molecular level.
Purpose of the Study:
- To investigate the conformational basis for the interaction between ABH active substances in saliva and LEWIS antigens on stomach epithelial cells.
- To explore the role of three-dimensional oligosaccharide structures in carbohydrate-receptor site interactions.
Main Methods:
- Chemical synthesis of LEWIS-d and LEWIS-b antigenic determinants.
- Inhibition assays using Ulex europaeus lectin and chemically modified H (Type 1) and H (Type 2) structures.
- Conformational analysis of oligosaccharide structures.
Main Results:
- Synthesized LEWIS-d and LEWIS-b determinants did not initially bind Ulex europaeus lectin.
- De-N-acetylated forms of these LEWIS determinants inhibited Ulex europaeus agglutination, indicating binding.
- Results suggest LEWIS-b and d antigens in saliva may exist in an amine form.
Conclusions:
- Conformational analysis is vital for understanding carbohydrate-receptor interactions.
- The findings provide insights into the potential presentation of LEWIS antigens in saliva.
- Further research is needed to confirm the presence of LEWIS antigens in the amine form in vivo.