Localization of neutral, magnesium-stimulated sphingomyelinase in plasma membrane of cultured neuroblastoma cells

Matthew W. Spence, Jan Wakkary, Joe T.R. Clarke, Harold W. Cook

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

Abstract

A parallel is shown between the distribution of neutral sphingomyelinase and plasma membrane enzymes (5′-nucleotidase and (Na+ + K+)-activated ATPase) in cultured neuroblastoma cells. In contrast there is no evidence of localization in lysosomes (β-hexosaminidase and acid sphingomyelinase), mitochondria (carnitine palmitoyltransferase), or cytosol. Activity in the microsomal fraction is attributed primarily to plasma membrane contamination.

Original languageEnglish
Pages (from-to)162-164
Number of pages3
JournalBiochimica et Biophysica Acta - General Subjects
Volume719
Issue number1
DOIs
Publication statusPublished - Oct 28 1982

Bibliographical note

Funding Information:
The authors acknowledge the expert technical assistance of Mr. Alfred Archibald and Mr. Robert Zwicker. This research was supported in part by a grant-in-aid from the Medical Research Council of Canada (PG-16). H.W.C. is a Scholar and M.W.S. is a Career Investigator of the Medical Research Council of Canada.

ASJC Scopus Subject Areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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