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Related Experiment Videos

Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase.

K Hjalmarsson, S L Marklund, A Engström

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1987
    PubMed
    Summary

    Researchers isolated and sequenced a human placenta cDNA clone for extracellular superoxide dismutase (EC-SOD). This secretory enzyme shares homology with other CuZn SODs, suggesting an evolutionary link and a heparin-binding domain.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Evolutionary Biology

    Background:

    • Extracellular superoxide dismutase (EC-SOD) is a crucial antioxidant enzyme.
    • Understanding EC-SOD's structure and evolutionary origins is important for its biological function.

    Purpose of the Study:

    • To isolate and determine the nucleotide sequence of a human placenta cDNA clone encoding EC-SOD.
    • To analyze the deduced amino acid sequence of EC-SOD for structural and functional insights.
    • To investigate the evolutionary relationship of EC-SOD with other superoxide dismutases.

    Main Methods:

    • cDNA library screening
    • Nucleotide sequencing
    • Amino acid sequence analysis
    • Homology comparisons with known superoxide dismutases

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    Main Results:

    • Isolated and sequenced a human placenta cDNA clone for EC-SOD.
    • EC-SOD is a secretory protein with a signal peptide and a mature enzyme of 222 amino acids.
    • The mature EC-SOD sequence shows significant homology to eukaryotic CuZn SODs, particularly in the active site region.
    • A distinct carboxyl-terminal region suggests heparin and heparan sulfate binding affinity.
    • Evolutionary analysis suggests EC-SOD diverged from CuZn SODs prior to the evolution of fungi and plants.

    Conclusions:

    • The human EC-SOD sequence provides insights into its structure, function, and secretory pathway.
    • EC-SOD likely evolved from CuZn SODs, with specific adaptations for its extracellular role and heparin binding.
    • The findings contribute to understanding the evolution and diversity of the superoxide dismutase family.