Dihydroxyacetone synthase is localized in the peroxisomal matrix of methanol-grown Hansenula polymorpha View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1985-12

AUTHORS

Anneke C. Douma, Marten Veenhuis, Wim de Koning, Melchior Evers, Wim Harder

ABSTRACT

The subcellular localization of dihydroxyacetone synthase (DHAS) in the methylotrophic yeast Hansenula polymorpha was studied by various biochemical and immunocytochemical methods. After cell fractionation involving differential and sucrose gradient centrifugation of protoplast homogenates prepared from methanol-grown cells, DHAS cosedimented with the peroxisomal enzymes alcohol oxidase and catalase. Electron microscopy of this fraction showed that it contained mainly intact peroxisomes, whereas SDS-polyacrylamide gel electrophoresis revealed two major protein bands (75 and 78 kDa) which were identified as alcohol oxidase and DHAS, respectively. The localization of DHAS in peroxisomes was further established by immunocytochemistry. After immuno-gold staining carried out on ultrathin sections of methanol-grown H. polymorpha using DHAS-specific antibodies, labelling was confined to the peroxisomal matrix. More... »

PAGES

237-243

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00411242

DOI

http://dx.doi.org/10.1007/bf00411242

DIMENSIONS

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