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Effect of Detergents on the Utilization of Sphingomyelin by Brain Sphingomyelinases

  • S. Gatt
  • T. Dinur
  • S. Yedgar
  • Z. Leibovitz-Ben Gershon
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 101)

Abstract

Complex lipids belonging to the group classified as “insoluble, swelling amphiphilic lipids” (1) form multibilayered liposomes when dispersed in aqueous media. These large aggregates are generally poor substrates for enzymatic utilization and, for interaction with suitable enzymes must be further dispersed or “solubilized”. This is usually done with the aid of a detergent (reviewed in ref. 2), although some success was obtained with sonicated, single-bilayered liposomes (e.g., 3). The exact nature of the effect, by the detergent that facilitates the interaction with the enzyme is still rather obscure. For numerous enzymatic reactions a nonionic detergent (e.g., Triton X-100) * or an anionic detergent (e.g., sodium dodecylsulfate or bile salts) was used; in some cases detergent mixtures were employed (2). It is generally assumed that the detergent exerts its beneficiary action by solubilizing the substrate. However, with some enzymes that utilize lipid substrates, a detergent enhanced reaction rates even when using a non-lipid, water-soluble substrate (e.g., (β-glucosidase using p-nitrophenyl glucoside (4) or methyl umbiliferyl glucoside (5). In such a case the detergent most probably affects the enzyme rather than the substrate. It is self-evident that if a lipid substrate (e.g., glucosyl-ceramide) is the substrate for the same enzyme, the detergent also solubilizes the substrate further to its affecting the enzyme.

Keywords

Bile Salt Mixed Micelle Aggregation Number Critical Micellar Concentration Sodium Taurocholate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • S. Gatt
    • 1
  • T. Dinur
    • 1
  • S. Yedgar
    • 1
  • Z. Leibovitz-Ben Gershon
    • 2
  1. 1.Laboratory of Neurochemistry, Department of BiochemistryHadassah University HospitalJerusalemIsrael
  2. 2.Hebrew University-Hadassah Medical School and the Pediatrics Research UnitHadassah University HospitalJerusalemIsrael

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