PMID: 1204609Nov 1, 1975Paper

Alcohol oxidase and catalase in peroxisomes of methanol-grown Candida boidinii

European Journal of Biochemistry
R RoggenkampF Wagner

Abstract

Microbodies, designated as peroxisomes because of their enzyme complement, have been isolated from methanol-grown cells of Candida boidinii. Spheroplast lysates were separated on non-continuous Ficoll density gradients, resulting in a mitochondrial fraction and a peroxisome fraction. Estimates of purity using the mitochondrial enzyme markers suggested that the contamination of mitochondria in the peroxisome fraction was about 2-3%. As shown by electron microscopy the peroxisomes were 0.4-0.6 mum in diameter and contained crystalloid inclusions. Alcohol oxidase and catalase, which catalyse the oxidation of methanol to formaldehyde in Candida boidinii, could be localized within the peroxisomes. Gel-electrophoretic studies of the peroxisome fraction demonstrated that it contained only two predominant protein bands consistent with alcohol oxidase and catalase. No alcohol oxidase and catalase activity was found in mitochondria.

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Citations

Feb 4, 1977·Archives of Microbiology·S KawamotoS Fukui
Jan 1, 1978·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·E Cardemil
Feb 1, 1978·European Journal of Biochemistry·S KawamotoS Fukui
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Aug 16, 2015·Applied Microbiology and Biotechnology·Lennart LeßmeierVolker F Wendisch
Oct 31, 2014·Proceedings of the National Academy of Sciences of the United States of America·Igor W BogoradJames C Liao
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May 15, 1992·FEMS Microbiology Letters·I KeizerM Veenhuis
Dec 1, 1976·Archives of Microbiology·J P van DijkenW Harder
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May 1, 1979·Archives of Biochemistry and Biophysics·R A Moreau, A H Huang
Sep 1, 1981·Archives of Biochemistry and Biophysics·R N PatelP Derelanko

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