Acid Sphingomyelinase from Human Urine: Purification and Characterisation View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1988

AUTHORS

L. E. Quintern , H. Nehrkorn , K. Sandhoff , G. Weitz , J. M. Tager , A. W. Schram

ABSTRACT

Acid sphingomyelinase (sphingomyelin phosphodiesterase, EC 3.1.4.12) was purified from human urine in the presence of 0.1 % Nonidet P-40. The activity could be enriched up to 30 000 fold by sequential chromatography on Octyl-Sepharose, Concanavalin-A Sepharose, Blue Sepharose and DEAE Cellulose. The last purification step yielded an enzyme preparation with a specific activity of about 2.5–10 mmol sphingomyelin cleaved/h per mg protein and with a yield of about 3–16 %. Purified sphingomyelinase appeared to be homogeneous in sodium dodecyl sulphate Polyacrylamide gel electrophoresis with a mass of about 70 kDa. In the presence of 0.08 % sodium taurodeoxycholate the preparation showed phosphodiesterase activity towards several phospholipids. Sphingomyelin, phosphatidylcholine, phosphatidylglycerol and at a slow rate phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine were hydrolysed. The phospholipase C activity towards phosphatidylcholine and phosphatidylglycerol and acid sphingomyelinase activity copurified during the entire purification procedure, indicating that acid sphingomyelinase has phospholipase C activity towards these lipids. Addition of 100 µM tripalmitoylglycerol to the assay system (which contains 100 µM sphingomyelin) instead of detergent, stimulated the reaction about 20-fold, thus offering a sensitive system for the assay of acid sphingomyelinase in a system free of detergents. Sphingomyelin degradation was strongly inhibited by phosphatidylinositol 4′, 5′-bis phosphate, adenosine 3′, 5′- diphosphate and adenine-9-β-D arabinofuranoside 5′-monophosphate (50 % inhibition at inhibitor concentrations of 1–5 µM and a substrate concentration of 100 µM sphingomyelin). More... »

PAGES

109-118

Book

TITLE

Lipid Storage Disorders

ISBN

978-1-4612-8300-3
978-1-4613-1029-7

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4613-1029-7_13

DOI

http://dx.doi.org/10.1007/978-1-4613-1029-7_13

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001498791


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