Volume 36, Issue 5 pp. 498-501
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Ornithine Decarboxylase and Trypanothione Reductase Genes in Leishmania braziliensis guyanensis

JANET S. KEITHLY

JANET S. KEITHLY

Division of International Medicine. Cornell University Medical College. New York, New York 10021

Laboratory of Parasitology, Wadswoth Center for Research, New York State Department of Health, Empire State Plaza, Albany, New York 12201.

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First published: September 1989
Citations: 2

ABSTRACT

. Ornithine decarboxylase and trypanothione reductase are the key enzymes in polyamine and trypanothione metabolism in kinetoplastids. Using a heterologous Trypanosoma brucei brucei probe for ornithine decarboxylase and a mixed synthetic probe of 29 oligonucleotides for trypanothione reductase, we have detected the putative genes for these enzymes by Southern blot hybridization using genomic DNA of Leishmania braziliensis guyanensis MHOM/SR/80/CUMC I. The trypanothione reductase probe was constructed both from the conserved codon usage of the redox active site for other flavin oxidoreductases over a wide evolutionary scale, and the preferred codon usage for other genes in species of Leishmania.

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