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Phosphoglycolate phosphatase. Purification and properties.

J T Christeller, N E Tolbert

    The Journal of Biological Chemistry
    |March 25, 1978
    PubMed
    Summary
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    Researchers purified phosphoglycolate phosphatase (an enzyme) from tobacco leaves, revealing it

    Area of Science:

    • Biochemistry
    • Plant Physiology

    Background:

    • Phosphoglycolate phosphatase (PGP) plays a role in photorespiration.
    • Understanding PGP's properties is crucial for plant metabolism research.

    Purpose of the Study:

    • To purify and characterize phosphoglycolate phosphatase from tobacco leaves.
    • To compare tobacco PGP with spinach PGP.

    Main Methods:

    • Acetone fractionation
    • DEAE-cellulose chromatography
    • Molecular sieve chromatography
    • Polyacrylamide gel electrophoresis
    • Isoelectric focusing
    • Sedimentation velocity
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis

    Related Experiment Videos

    Main Results:

    • PGP was purified 1500-fold to 90-95% homogeneity.
    • The native enzyme has a molecular weight of approximately 80,500-86,300 Da and is a tetramer.
    • The isoelectric point (pI) is 3.8-3.9.
    • Tobacco PGP is more stable than spinach PGP and is not inactivated by lipase.
    • Citrate or isocitrate stabilized the enzyme.
    • Ribose 5-phosphate competitively inhibited the enzyme.

    Conclusions:

    • Tobacco phosphoglycolate phosphatase is a stable tetrameric enzyme.
    • Citrate/isocitrate stabilize the enzyme, and ribose 5-phosphate is a competitive inhibitor.