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Adenosine triphosphatase activities in Trypanosoma cruzi.

作者信息

Frasch A C, Segura E L, Cazzulo J J, Stoppani A O

机构信息

Instituto de Química Biológica, Facultad de Medicina, Universidad de Buenos Aires, Argentina.

出版信息

Comp Biochem Physiol B. 1978;60(3):271-5. doi: 10.1016/0305-0491(78)90100-1.

DOI:10.1016/0305-0491(78)90100-1
PMID:162583
Abstract
  1. Subcellular fractions obtained from epimastigotes of Trypanosoma cruzi, disrupted by three different procedures, contained in addition to the already known Mg2+-activated adenosine triphosphatase (ATPase; E.C.3.6.1.4), a Ca2+-ATPase activity. 2. The Ca2+-ATPase (a) was activated by low concentrations of CaCl2 (apparent Ka, 80 microM); (b) had a Km for ATP of 0.6 mM (at 1 mM CaCl2, pH 8.0); (c) presented a broad pH curve (optimum 7.1-8.6); and (d) was insensitive to oligomycin concentrations which inhibited the Mg2+-ATPase present in the same preparations. 3. All attempts to find a (Na+-K+)-activated, ouabain-inhibited, ATPase have been unsuccessful, in spite of the fact that living epimastigoes of T. cruzi are able to concentrate K+ and exclude Na+ from the medium.
摘要

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