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Related Experiment Videos

Microheterogeneity in yeast invertase.

W J Colonna, F R Cano, J O Lampen

    Biochimica Et Biophysica Acta
    |March 28, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Yeast external invertase contains covalently bound phosphate, with varying mannose/PO4 ratios. This phosphoinvertase heterogeneity is linked to increased mannan and phosphate content, not enzyme activity.

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    Area of Science:

    • Biochemistry
    • Glycobiology
    • Enzymology

    Background:

    • Yeast external invertase is a glycoenzyme composed of protein and mannan.
    • Covalently bound phosphate has been identified within yeast external invertase preparations.
    • Understanding the composition and heterogeneity of this enzyme is crucial for its functional characterization.

    Purpose of the Study:

    • To investigate the presence and extent of covalently bound phosphate in yeast external invertase.
    • To determine the relationship between phosphate content, mannan composition, and enzyme heterogeneity.
    • To explore the factors contributing to the microheterogeneity of phosphoinvertase.

    Main Methods:

    • Analysis of mannose/PO4 ratios in different yeast invertase preparations.

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  • Quantification of phosphorus as mannose 6-phosphate.
  • Enzyme characterization using electrofocusing and hydroxyapatite chromatography.
  • Comparison with cell wall mannans and internal invertase.

    • Main Results:

    • Yeast external invertase preparations exhibited varying mannose/PO4 ratios, indicating diverse phosphorylation levels.
    • Approximately 69% of the phosphorus was recovered as mannose 6-phosphate in one high-PO4 enzyme.
    • Phosphorylation levels did not correlate with invertase activity, and were higher than in cell wall mannans.
    • Electrofocusing and chromatography revealed significant microheterogeneity in phosphoinvertase, with multiple isozymes.
    • This heterogeneity was attributed to variations in mannan and phosphate content, not activity.

    Conclusions:

    • Yeast external invertase is a phosphoglycoenzyme with significant microheterogeneity.
    • The observed heterogeneity is primarily driven by variations in mannan and covalently bound phosphate content.
    • Contamination by cell wall phosphomannan is unlikely to be the source of phosphate in the enzyme.