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Related Experiment Videos

Characterization of MOPC 315 IgA oligosaccharide processing intermediates.

S Hickman, J L Theodorakis

    Biochemical and Biophysical Research Communications
    |April 30, 1985
    PubMed
    Summary
    This summary is machine-generated.

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    This study characterized oligosaccharide structures on MOPC 315 IgA, revealing an ordered removal of alpha 1,2-linked mannose residues. This provides insight into the processing of N-linked glycans on murine immunoglobulin heavy chains.

    Area of Science:

    • Glycobiology
    • Immunology
    • Structural Biology

    Background:

    • Asparagine-linked oligosaccharides undergo complex processing in the Golgi apparatus.
    • Understanding glycan structures is crucial for immunoglobulin function and immune response.

    Purpose of the Study:

    • To characterize the alpha 1,2-mannose containing oligosaccharide structures on the alpha-chain of MOPC 315 IgA.
    • To investigate the sequence of mannose residue removal during glycan processing.

    Main Methods:

    • Enzymatic digestion using specific glycosidases.
    • Chemical modification via acetolysis.
    • Structural analysis of oligosaccharides.

    Main Results:

    • Identified Man6GlcNAc2 as a single isomeric structure, a substrate for Golgi alpha 1,2-mannosidase.

    Related Experiment Videos

  • Determined Man7-9GlcNAc2 structures as single isomers.
  • Demonstrated an ordered sequence of alpha 1,2-linked mannose removal.

    • Conclusions:

    • The processing of N-linked glycans on the MOPC 315 IgA heavy chain follows a highly ordered pathway.
    • Specific mannosidase activities dictate the sequential removal of mannose residues.
    • Elucidates the structural basis for N-glycan maturation in murine myeloma IgA.