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Related Experiment Videos

The primary structure of allergen M from cod.

S Elsayed, H Bennich

    Scandinavian Journal of Immunology
    |January 1, 1975
    PubMed
    Summary

    The primary structure of cod allergen M was determined, revealing its full amino acid sequence and a single glucose residue. This allergen shows limited homology with related fish proteins, suggesting potential cross-reactivity.

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    Area of Science:

    • Biochemistry
    • Immunology
    • Molecular Biology

    Background:

    • Allergen M is a major cod allergen.
    • Understanding its structure is crucial for diagnosing and managing fish allergies.

    Purpose of the Study:

    • To determine the complete primary structure of cod allergen M.
    • To analyze its homology with other fish allergens.
    • To investigate the nature of its glycosylation.

    Main Methods:

    • Dansyl-Edman degradation for NH2-terminal peptide sequencing.
    • Summation of sequence data from TM1 and TM2 fragments.
    • Homology analysis using sequence data.
    • Gas chromatography for analyzing glycosidic bonds.

    Main Results:

    • The complete amino acid sequence of cod allergen M (113 residues, 12,328 Da) was elucidated.
    • Fragment TM1 (75 amino acids, 8,492 Da) contains one glucose residue.
    • Cod allergen M shows 34.5% homology with other fish allergens.
    • A single blocked half-cystine was identified.
    • Glucose is likely bound to Cys 18 via an S-glucosidic bond.

    Conclusions:

    • The primary structure of cod allergen M is now fully characterized.
    • The identified glycosylation and homology provide insights into its allergenic potential and cross-reactivity.

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