Purification and Properties of Acid Sphingomyelinase from Human Urine

  • G. Weitz
  • L. E. Quintern
  • A. W. Schram
  • J. A. Barranger
  • J. M. Tager
  • K. Sandhoff
Part of the NATO ASI Series book series (NSSA, volume 116)


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.


Human Urine Acid Sphingomyelinase Urinary Enzyme High Molecular Weight Component Lysosomal Accumulation 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • G. Weitz
    • 1
  • L. E. Quintern
    • 1
  • A. W. Schram
    • 2
  • J. A. Barranger
    • 3
  • J. M. Tager
    • 2
  • K. Sandhoff
    • 1
  1. 1.Institute of Organic Chemistry and BiochemistryUniversity of BonnBonnFederal Republic of Germany
  2. 2.Laboratory of BiochemistryUniversity of AmsterdamAmsterdamThe Netherlands
  3. 3.Developmental and Metabolic Neurology Branch, National Institute of Neurological and Communicative Diseases and StrokeNational Institutes of HealthBethesdaUSA

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