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Archives of Microbiology

, Volume 105, Issue 1, pp 261–267 | Cite as

Cytochemical localization of catalase activity in methanol-grown Hansenula polymorpha

  • J. P. Van Dijken
  • M. Veenhuis
  • C. A. Vermeulen
  • W. Harder
Short Communications

Abstract

The localization of peroxidase activity in methanol-grown cells of the yeast Hansenula polymorpha has been studied by a method based on cytochemical staining with diaminobenzidine (DAB). The oxidation product of DAB occurred in microbodies, which characteristically develop during growth on methanol, and in the intracristate space of the mitochondria.

The staining of microbodies was H2O2 dependent, appeared to be optimal at pH 10.5, diminished below pH 10 and was inhibited by 20 mM 3-amino 1,2,4 triazole (AT). In contrast to these observations, the reaction in the mitochondria was not H2O2 dependent and not notably affected by differences in pH in the range of 8.5 to 10.5. Microbodies and mitochondria were also stained when H2O2 was replaced by methanol. Appropriate control experiments indicated that in this case methanol oxidase generated the H2O2 for the peroxidative conversion of DAB by catalase. These results suggest that catalase is located in the microbodies of methanol-grown yeasts. A model for a possible physiological function of the microbodies during growth on methanol is put forward.

Key words

Methanol Yeasts Microbodies Diaminobenzidine Catalase Methanol oxidase Hanseula polymorpha 

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Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • J. P. Van Dijken
    • 1
    • 2
  • M. Veenhuis
    • 1
    • 2
  • C. A. Vermeulen
    • 1
    • 2
  • W. Harder
    • 1
    • 2
  1. 1.Department of Microbiology Biological CentreUniversity of GroningenHaren (Gr.)
  2. 2.Department of Electron Microscopy, Biological CentreUniversity of GroningenHaren (Gr.)

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