Two Heat-Stable Low-Molecular-Mass Proteins Stimulating the Enzymic Sphingomyelin Degradation Isolated from Human Gaucher and Normal Spleen
A few years ago we have reported that Gaucher and normal spleen contain a heat-stable non-enzymic protein fraction stimulating the enzymic degrada-tion of the lipids sphingomyelin and glucosylceramide in the absence of detergents1. However, this activator fraction did not stimulate ß-glucosidase activity towards the watersoluble fluorogenic substrate. It could be therefore assumed that this activator was not identical with the one reported by Ho and O’Brien2 or Berent and Raclin3. Our results were based on crude heat-treated extracts of Gaucher spleen which were further enriched by ion-exchange chromatography and isoelectrofocusing. It was not possible with these procedures to separate an activator for glucosylceramide degradation from another one responsible only for sphingomyelin degradation.
KeywordsGauche Disease Lysosomal Storage Disease Normal Spleen Octyl Glucoside Myelin Degradation
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