English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Two activator proteins for sphingomyelin degradation were isolated from heat-treated extracts of human Gaucher spleen. The separation was based on the degree of affinity of the activators for ConA-Sepharose. Activator A1, which had affinity for ConA-Sepharose, was purified 1 430-fold, and activator A2, which had no affinity for ConA-Sepharose, 2 140-fold as compared with the original heat-treated extracts. The molecular masses of activator A1 and activator A2 were 6 000 and 3 500 Da, respectively, as determined by dodecyl sulfate electrophoresis, and approximately 5 000 Da as measured in the presence of 8M urea. The two activators had similar properties and a similar but not identical amino-acid composition. Both were shown to form a complex with sphingomyelin and stimulate the degradation of sphingomyelin by normal fibroblast homogenates and by an approximately 1 430-fold purified sphingomyelin phosphodiesterase ("acid sphingomyelinase") from normal human urine. This stimulation was greatly reduced after incubation with pronase E. The enzymic degradation of glucosylceramide and galactosylceramide was not affected by these activators.

Isolation of two Forms of an Activator Protein for the Enzymic Sphingomyelin Degradation from Human Gaucher Spleen