The Activity of Parafusin Is Distinct from That of Phosphoglucomutase in the Unicellular Eukaryote Paramecium

Anders P. Andersen, Elzbieta Wyroba, Milaniya Reichman, Hong Zhao, Brgit H. Satir

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

In this paper we identified the presence of a Paramecium phosphoglucomutase enzymatic activity which is clearly distinct from that of parafusin - the exocytosis-related phosphoglycoprotein. Since the recently cloned parafusin showed homology to rabbit muscle phosphoglucomutase, we have designed a specific peptide parafusin antibody - generated to a region not present in any known sequenced phosphoglucomutases - to distinguish parafusin from the Paramecium phosphoglucomutase. Separation of these two proteins was obtained using liquid chromatography, enzymatic activity assay and immunoblotting analysis with the specific parafusin peptide antibody. Parafusin fractions incorporated [β35S]UDP-Glc but not [35S]Glc-1-P, whereas Paramecium phosphoglucomutase fractions incorporated [35S]Glc-1-P but not [β35S]UDP-Glc. This indicates that these two proteins are separate entities exhibiting different properties and most likely distinct functions in the cell.

Original languageEnglish (US)
Pages (from-to)1353-1358
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume200
Issue number3
DOIs
StatePublished - May 15 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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