Import of peroxisomal hydroxypyruvate reductase into glyoxysomes

Christof Sautter, Eva Sautter, Bertold Hock

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


A new procedure was used to purify the peroxisomal matrix enzyme hydroxypyruvate reductase (HPR) from green leaves of pumpkin (Cucurbita pepo L.) and spinach (Spinacia oleracea L.). Monospecific antibodies were prepared against this enzyme in rabbits. Immunoprecipitation of HPR from watermelon (Citrullus vulgaris Schrad.) yielded a single protein with a subunit molecular weight of 45 kDa. Immunohistochemical labeling of HPR was found exclusively in watermelon microbodies. Isolated polyadenylated mRNA from light-grown watermelon cotyledons was injected into Xenopus laevis oocytes. The heterologous in-vivo translation product of HPR exhibited the same molecular weight as the immunoprecipitate from watermelon cotyledons, indicating the lack of a cleavable extra sequence. The watermelon HPR translated in oocytes was imported into isolated glyoxysomes from castor bean (Ricinus communis L.) endosperm and remained resistant to proteolysis after the addition of proteinase K. The HPR did not change its apparent molecular weight during sequestration; however, it may have changed its conformation.

Original languageEnglish
Pages (from-to)149-158
Number of pages10
Issue number2
StatePublished - Nov 1988


  • Citrullus
  • Hydroxypyruvate reductase
  • Microbody biogenesis
  • Riclnus
  • Xenopus (oocytes)


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