Canine neutrophil plasma membrane markers

Robert T O'Donnell, Burton R. Andersen

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


The purpose of this investigation was to determine which enzyme activities are true canine neutrophil plasma membrane markers. Three enzymes thought to be present on plasma membranes were chosen for study: 5′-nucleotidase, magnesium-dependent adenosine triphosphatase (Mg2+-ATPase), and leucine aminopeptidase. Both 5′-nucleotidase and Mg2+-ATPase were found to be ectoenzymes in the canine neutrophil but additional Mg2+-ATPase activity was located intracellularly. An endogenous inhibitor of 5′-nucleotidase was found in the cytosol of canine neutrophils. The specific 5′-nucleotidase inhibitor, adenosine 5′-[α,β-methylene] diphosphate also inhibited the canine enzyme in intact cells. Leucine aminopeptidase was located solely in the myeloperoxidase-containing granules of the canine neutrophil. Plasma membrane, as identified by the presence of Mg2+-ATPase and 5′-nucleotidase activities, was separated from other cell organelles by Percoll-density gradient centrifugation of a 10 000 X g supernatant of nitrogen cavitated neutrophils.

Original languageEnglish (US)
Pages (from-to)307-312
Number of pages6
JournalBBA - Biomembranes
Issue number2
StatePublished - Apr 11 1985
Externally publishedYes


  • (Canine)
  • 5′-Nucleotidase
  • Mg-ATPase
  • Neutrophil membrane
  • Plasma membrane marker

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology


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