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Adenosine triphosphatase activity of Tritrichomonas foetus

Lloyd, David, Lindmark, Donald G. and MÜLLER, MIKLÓS 1979. Adenosine triphosphatase activity of Tritrichomonas foetus. Microbiology 115 (2) , pp. 301-307. 10.1099/00221287-115-2-301

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Abstract

Homogenates of Tritrichomonas foetus exhibited a Mg2+-dependent adenosine triphosphatase (ATPase) activity, with a pH optimum in Tris buffers of 8.2 to 8.3. The activity was not sensitive to oxygen. At high concentrations, quercetin and 4-chloro-7-nitrobenzofurazan inhibited ATPase activity in the cytoplasmic extract by 20 and 70%, respectively, whereas oligomycin, venturicidin, triethyltin, leucinostatin, dibutylchloromethyltin chloride, spegazzinine, efrapeptin, citreoviridin and sodium azide had no effect and N,N'-dicyclohexylcarbodi-imide stimulated the activity somewhat. The activity was localized in a population of small cytoplasmic particles which also contained an acid phosphatase. There was no indication of an association of ATPase with hydrogenosomes. The ATPase activity (or activities) in this aerotolerant anaerobe is different from the ATPases characteristic of mitochondria or of anaerobic bacteria.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Microbiology Society
ISSN: 1350-0872
Last Modified: 05 Mar 2020 12:15
URI: http://orca.cardiff.ac.uk/id/eprint/127799

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