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sphingomyelin/brassica

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5 results

Pseudomonas aeruginosa cytotoxin: the influence of sphingomyelin on binding and cation permeability increase in mammalian erythrocytes.

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A cytotoxic protein isolated from Pseudomonas aeruginosa damages the plasma membranes of many mammalian cells by forming pores. We studied binding of the 125I-cytotoxin and the resulting increase of cation permeability in erythrocytes of various mammalian species. The sensitivity of red blood cells

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin.

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GM2 activator protein (GM2AP) is a specific protein cofactor that stimulates the enzymatic hydrolysis of the GalNAc from GM2, a sialic acid containing glycosphingolipid, both in vitro and in lysosomes. While phospholipids together with glycosphingolipids are important membrane constituents, little

Enzymic assay for lecithin in amniotic fluid.

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We describe an enzymic method for determining lecithin in amniotic fluid. Phospholipase D from savoy cabbage is used to liberate choline from lecithin, and the liberated choline is oxidized to betaine and hydrogen peroxide by choline oxidase from Arthrobacter globiformis. The hydrogen peroxide forms

Identification of a sphingolipid-specific phospholipase D activity associated with the generation of phytoceramide-1-phosphate in cabbage leaves.

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The structure and biosynthetic route for an unidentified lipid (lipid X) detected by TLC of cabbage (Brassica oleracea) lipids was determined. Lipid X is a phospholipid that is resistant to mild alkali and detectable by MALDI-TOF MS as an adduct with Phos-tag, a phosphate-capture zinc complex.

Organization of phospholipids in human red cell membranes as detected by the action of various purified phospholipases.

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1. The action of eight purified phospholipases on intact human erythrocytes has been investigated. Four enzymes, e.g. phospholipases A2 from pancreas and Crotalus adamanteus, phospholipase C from Bacillus cereus, and phospholipase D from cabbage produce neither haemolysis nor hydrolysis of
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