Abstract
Cleavage by the GPI-PLD provides definitive evidence of a minimal GPI structure: glucosamine-phosphatidylinositol. Unlike the case for PI-PLC, cleavage by the GPI-PLD is unaffected by acylation of the inositol ring. Thus the GPI-PLD provides an excellent simple enzymatic tool for analyzing the basic core structure of GPI anchors.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Acylation
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Animals
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Carbohydrate Conformation
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Carbohydrate Sequence
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Cations, Divalent / pharmacology
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Cattle
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Chromatography, Affinity / methods
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Chromatography, Gel / methods
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Chromatography, Ion Exchange / methods
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Cloning, Molecular / methods
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DNA, Complementary
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Detergents / pharmacology
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Electrophoresis, Polyacrylamide Gel / methods
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Escherichia coli
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Gene Expression
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Glucosamine / analysis
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Glycosylphosphatidylinositols / chemistry*
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Humans
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Kinetics
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Mammals
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Molecular Conformation
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Molecular Sequence Data
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Molecular Weight
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Phospholipase D / blood*
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Phospholipase D / chemistry
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Phospholipase D / isolation & purification*
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Phosphorylation
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Recombinant Proteins / chemistry
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Substrate Specificity
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Ultracentrifugation / methods
Substances
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Cations, Divalent
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DNA, Complementary
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Detergents
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Glycosylphosphatidylinositols
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Recombinant Proteins
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Phospholipase D
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glycoprotein phospholipase D
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Glucosamine