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Related Experiment Videos

An enzyme basis for blood type A intermediate status.

A Yoshida, V Davé, D R Branch

    American Journal of Human Genetics
    |November 1, 1982
    PubMed
    Summary

    Blood type A is subclassified into A1, A2, and A1-A2 intermediate (Aint) based on red cell agglutination. Aint individuals have unique enzymes affecting blood group H-site glycosylation and A/H activity.

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    Area of Science:

    • Immunology
    • Biochemistry
    • Genetics

    Background:

    • Blood type A exhibits variations including A1, A2, and A1-A2 intermediate (Aint) phenotypes.
    • These variations are determined by red blood cell agglutinability using anti-A1 and anti-H lectins.
    • Erythrocyte membranes in Aint individuals show significant unglycosylated blood group H-sites (approx. 80%).

    Purpose of the Study:

    • To investigate the biochemical differences in blood group GalNAc transferases among A1, A2, and Aint phenotypes.
    • To correlate enzyme activity with glycosylation patterns and A/H antigen expression on red blood cells.

    Main Methods:

    • Analysis of red cell agglutinability with anti-A1 and anti-H lectins.
    • Characterization of plasma-derived blood group GalNAc transferase (UDP-GalNAc:2'-fucosylgalactoside-alpha-3-N-acetylgalactosaminyl transferase) activity.
    • Assessment of substrate affinities (UDP-GalNAc and 2'-fucosyllactose) for the enzymes from different blood types.

    Main Results:

    • Aint plasma contains a distinct GalNAc transferase with high affinity for UDP-GalNAc but very low affinity for 2'-fucosyllactose.
    • A1 enzyme shows high affinity for both UDP-GalNAc and 2'-fucosyllactose.
    • A2 enzyme exhibits low affinity for both substrates.
    • The low affinity of Aint-enzyme for H-substance analogs contributes to reduced A activity and increased H activity in Aint red cells.

    Conclusions:

    • The blood group A allele is subdivided into A1, A2, and Aint alleles.
    • Each allele encodes a specific blood group GalNAc transferase with differential substrate affinities.
    • Enzyme characteristics explain the observed differences in glycosylation and antigen activity in Aint erythrocytes.

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