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Determination of measles virus protein molecular weights on high percentage, highly cross-linked SDS polyacrylamide

M J Carter, K Baczko

    Zeitschrift Fur Naturforschung. Section C, Biosciences
    |September 1, 1983
    PubMed

    Insights

    Measles virus research reveals a size discrepancy in membrane protein mRNA. This finding confirms a true biological phenomenon, not an artifact of measurement techniques.

    Area of Science:

    • Virology
    • Molecular Biology
    • Biochemistry

    Background:

    • Previous studies on measles virus mRNA indicated expected sizes for nucleocapsid and haemagglutinin messengers.
    • A significant size discrepancy was noted for the membrane protein mRNA, being approximately 50% larger than anticipated based on its protein product.

    Purpose of the Study:

    • To investigate the observed size discrepancy in measles virus membrane protein mRNA.
    • To determine if the discrepancy is a true biological phenomenon or an artifact of protein size determination methods, specifically related to SDS-polyacrylamide gel electrophoresis and hydrophobic molecule binding.

    Main Methods:

    • Analysis of measles virus mRNA molecule sizes.
    • Determination of measles virus matrix protein molecular weight using SDS-polyacrylamide gel electrophoresis.
    • Evaluation of potential underestimation of hydrophobic protein sizes due to increased SDS binding.

    Main Results:

    • The mRNA for measles virus membrane protein is confirmed to be approximately 50% larger than required for its protein product.
    • Measles virus membrane protein does not exhibit anomalous behavior during molecular weight determination via SDS-PAGE that would explain the size discrepancy.
    • The size discrepancy between measles virus membrane protein mRNA and its protein product is a genuine biological phenomenon.

    Conclusions:

    • The larger size of measles virus membrane protein mRNA is a true biological characteristic.
    • The discrepancy is not an artifact caused by the methodology used for determining the size of hydrophobic matrix proteins.

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