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A human cold agglutinin which binds lacto-N-neotetraose
Journal of Immunology (Baltimore, Md. : 1950)
|September 1, 1976
Summary
Researchers isolated a human cold agglutinin (McC) from Waldenström's macroglobulinemia serum. This IgM antibody specifically targets a unique carbohydrate sequence found on certain red blood cells.
Area of Science:
- Immunology
- Biochemistry
- Hematology
Background:
- Cold agglutinins are antibodies that bind to red blood cells at cold temperatures.
- Waldenström's macroglobulinemia is a rare cancer affecting B cells, often associated with abnormal antibody production.
Purpose of the Study:
- To isolate and characterize a specific human cold agglutinin (McC) from a patient with Waldenström's macroglobulinemia.
- To determine the specific carbohydrate structure recognized by the McC agglutinin.
Main Methods:
- Affinity chromatography using fixed erythrocyte stroma.
- Testing agglutinin reactivity with various human erythrocyte types (adult, cord, Oh, Oi).
- Ficin treatment to assess cell surface changes.
- Inhibition studies to identify the target carbohydrate sequence.
Main Results:
- Isolation of an IgM K cold agglutinin (McC).
- McC exhibited differential reactivity with erythrocytes, binding strongly to cord and Oh/Oi cells.
- Ficin treatment enhanced reactivity across all cell types.
- Inhibition studies identified the terminal carbohydrate sequence Gal(beta)1-4GlcNAc(beta)1-3Gal as the target.
Conclusions:
- The isolated McC agglutinin is specific for the Gal(beta)1-4GlcNAc(beta)1-3Gal carbohydrate structure.
- This finding provides insights into the molecular basis of cold agglutinin specificity in Waldenström's macroglobulinemia.
- Characterization of McC contributes to understanding immune responses and red blood cell interactions.