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Microsomal glutathione transferase. Primary structure.

R Morgenstern, J W DePierre, H Jörnvall

    The Journal of Biological Chemistry
    |November 15, 1985
    PubMed
    Summary
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    Researchers determined the primary structure of rat liver microsomal glutathione transferase, revealing a 154-residue amino acid sequence. This sequence provides insights into the enzyme

    Area of Science:

    • Biochemistry
    • Proteomics
    • Enzymology

    Background:

    • Microsomal glutathione transferase is a key enzyme in cellular detoxification.
    • Understanding its primary structure is crucial for elucidating its function and interactions.

    Purpose of the Study:

    • To determine the complete amino acid sequence of rat liver microsomal glutathione transferase.
    • To identify key structural features, including hydrophobic regions and secondary structures, relevant to membrane association and function.

    Main Methods:

    • Protein fragmentation using cyanogen bromide (CNBr) and proteolytic enzymes (e.g., staphylococcal protease, pepsin).
    • Amino acid sequencing via sequenator degradation and manual dimethylaminoazobenzene isothiocyanate (DABITC) method.
    • Analysis of hydrophobic segments and prediction of beta-strand secondary structures.

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    Main Results:

    • A 154-residue amino acid sequence for rat liver microsomal glutathione transferase was deduced.
    • The N-terminal alanine residue has a free alpha-amino group.
    • Cysteine at position 49 is involved in enzyme activation by sulfhydryl reagents.
    • Identified three regions with predicted beta-strand secondary structures and significant hydrophobic segments, particularly in the C-terminal half, suggesting roles in membrane interaction.

    Conclusions:

    • The determined primary structure provides a foundation for understanding the enzyme's catalytic mechanism and membrane integration.
    • Specific hydrophobic regions and predicted secondary structures are likely critical for the enzyme's association with the endoplasmic reticulum membrane.
    • No evidence of micro-heterogeneity was found, indicating a homogeneous protein population.