Saposin D: a sphingomyelinase activator

S Morimoto, B M Martin, Y Kishimoto, J S O'Brien

Research output: Contribution to journalArticlepeer-review

109 Citations (Scopus)


Saposin D, a newly discovered heat-stable, 10 kDa glycoprotein, was isolated from Gaucher spleen and purified to homogeneity. Chemical sequencing from its amino terminus demonstrated colinearity between its amino acid sequence and the deduced amino acid sequence of the fourth domain of prosaposin, the precursor of saposin proteins. Saposin D specifically stimulates acid sphingomyelinase but has no significant effect on the other hydrolases tested.

Original languageEnglish
Pages (from-to)403-10
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Oct 14 1988


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