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Barley leaf peroxidase: purification and characterization.

K Saeki, O Ishikawa, T Fukuoka

    Journal of Biochemistry
    |February 1, 1986
    PubMed
    Summary

    Researchers purified seven barley leaf peroxidase components with similar molecular weights. Differences in isoelectric points were attributed to glycosyl residues, not true isoenzymes.

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    Area of Science:

    • Biochemistry
    • Plant Science

    Background:

    • Peroxidases are crucial enzymes in plants.
    • Barley leaf extracts contain multiple peroxidase components.

    Purpose of the Study:

    • To purify and characterize the different peroxidase components from barley leaves.
    • To investigate the nature of these components, particularly their isoenzymes.

    Main Methods:

    • Enzyme purification using acetone fractionation, ammonium sulfate precipitation, ion-exchange chromatography (CM-cellulose, DEAE-Sepharose CL-6B), and molecular-sieve chromatography (Ultrogel AcA44).
    • Separation of components by isoelectric electrophoresis.
    • Characterization using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, spectrophotometry, and amino acid analysis.

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    Main Results:

    • Seven peroxidase components with identical molecular weights (44,000) were isolated.
    • Components exhibited distinct isoelectric points (pI) ranging from 6.3 to 9.3.
    • Amino acid analysis suggested differences in glycosyl residues, not true isoenzymes, account for varying pI values.

    Conclusions:

    • Barley leaf peroxidases consist of multiple components with similar molecular weights but different pI values.
    • Glycosylation is likely responsible for the observed charge heterogeneity.
    • The pI 9.3 component was successfully crystallized.