Localization and biochemical characterization of acid phosphatase isoforms in the olfactory system of adult rats

I. Krizbai, F. Joó, A. Pestean, J. Preil, H. Bötcher, J. R. Wolff

Research output: Contribution to journalArticle

5 Citations (Scopus)


Localization of acid phosphatases was studied with the use of β-glycerophosphate and p-nitrophenyl phosphate as substrates in the brain with special emphasis on the olfactory system of adult rat at light and electron microscopic level. With the use of β-glycerophosphate, a selective substrate for the lysosomal acid phosphatase, lead-containing reaction product was found in primary and secondary lysosomes of neurons, glial cells and perivascular macrophages as well as in the cytoplasm of olfactory sensory axons. Incubation with p-nitrophenyl phosphate as substrate additionally revealed a cytoplasmic isoform of acid phosphatase, which could not be inhibited by tartrate or fluoride and was predominantly located in dendrites. Acid phosphatase isoforms were biochemically characterized in samples prepared separately from the olfactory mucosa, olfactory nerve layer, olfactory bulb and its dendrodendritic synaptosomes isolated by subcellular fractionation. In the olfactory mucosa and olfactory nerve layer the lysosomal type (high molecular weight form) was the most prominent acid phosphatase form, whereas the isoform located in dendrites corresponded to the tartrate-resistant extralysosomal, cytosolic type (low molecular weight form). The functional significance of different isoforms of acid phosphatase in the olfactory sensory axons and dendritic elements is discussed.

Original languageEnglish
Pages (from-to)799-807
Number of pages9
Issue number3
Publication statusPublished - Dec 11 1996



  • acid phosphatase
  • histochemistry
  • molecular forms
  • olfactory system
  • plasticity

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this