Purification and Properties of Acid Sphingomyelinase from Human Urine View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1986

AUTHORS

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

ABSTRACT

Lysosomal sphingomyelinase catalyses the hydrolyses of the membrane lipid sphingomyelin to ceramide and phosphorylcholine. Deficiency of this enzyme, as is the case in patients suffering from Niemann-Pick disease type A or B, leads to the lysosomal accumulation of spingomyelini. In another group of Niemann-Pick patients (types C, D and E) the level of acid sphingomyelinase activity appears to be essentially normal or close to normal1. However, spingomyelin accumulates, but in modest amounts, together with other glycoshingolipids and cholesterol1. Until now there has been no satisfactory explanation for the biochemical defect underlying these forms of the disease. More... »

PAGES

261-265

Book

TITLE

Enzymes of Lipid Metabolism II

ISBN

978-1-4684-5214-3
978-1-4684-5212-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4684-5212-9_36

DOI

http://dx.doi.org/10.1007/978-1-4684-5212-9_36

DIMENSIONS

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