Phase partitioning detects differences between phospholipase-released forms of alkaline phosphatase--a GPI-linked protein.

F D Raymond; D W Moss; D Fisher

doi:10.1016/0304-4165(93)90125-r

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Phase partitioning detects differences between phospholipase-released forms of alkaline phosphatase--a GPI-linked protein.

F D Raymond·D W Moss·D Fisher

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Abstract

A number of enzymes are known to release alkaline phosphatase and other glycan phosphatidylinositol-anchored proteins from membrane surfaces. We describe a novel approach to detect and measure these activities by partitioning in aqueous phase systems. The procedures avoid the complications of micelle-formation involving hydrophobic molecules that may arise with detergent-based partition systems and can clearly distinguish between inositol-specific phospholipase C and D activities.

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Alkaline Phosphatase Bacillus cereus Dextrans Glycosylphosphatidylinositols Humans Isoenzymes Phosphatidylinositol Diacylglycerol-Lyase Phospholipase D Phosphoric Diester Hydrolases Placenta Polyethylene Glycols Solubility Streptomyces Type C Phospholipases Journal Article

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F D Raymond, D W Moss, D Fisher. 1993-02-13. Phase partitioning detects differences between phospholipase-released forms of alkaline phosphatase--a GPI-linked protein.. https://doi.org/10.1016/0304-4165(93)90125-r

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