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Related Experiment Videos

Tools to cleave glycoproteins

A Mellors1, D R Sutherland

  • 1Department of Chemistry and Biochemistry, University of Guelph, Ontario, Canada.

Trends in Biotechnology
|January 1, 1994
PubMed
Summary
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Enzymes cleave glycoproteins for analysis, aiding in glycosylation site determination and glycan release. A specific protease enables O-sialoglycoprotein identification and stem cell selection.

Area of Science:

  • Biochemistry
  • Glycobiology
  • Proteomics

Background:

  • Glycoproteins are crucial biomolecules with diverse functions.
  • Enzymatic cleavage is essential for analyzing glycoprotein structure and function.
  • Existing enzymes offer broad specificity for glycoprotein analysis.

Purpose of the Study:

  • To highlight the utility of various enzymes in glycoprotein analysis.
  • To introduce a specific protease for O-sialoglycoprotein identification.
  • To present an improved method for stem cell selection using enzymatic properties.

Main Methods:

  • Utilizing enzymes with specificity for carbohydrate-carbohydrate linkages, carbohydrate-protein bonds, and peptide backbones.
  • Employing a protease specific for O-sialoglycoproteins.

Related Experiment Videos

  • Applying immunomagnetic selection for human bone-marrow stem cells.

    • Main Results:

    • Enzymes facilitate the determination of glycosylation sites and release of glycan structures.
    • The identified protease specifically targets O-sialoglycoproteins, enabling epitope mapping.
    • The protease's low cytotoxicity and narrow specificity improve stem cell selection.

    Conclusions:

    • Enzymatic cleavage is a versatile tool in glycoprotein research.
    • A novel protease offers precise O-sialoglycoprotein identification.
    • This enzyme provides a superior method for immunomagnetic selection of stem cells.