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Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes Biol. Res.
UZCANGA,GRACIELA; GALÁN-CARIDAD,JOSÉ MANUEL; SUAREZ,KAREM NORIS; BUBIS,JOSÉ.
Trypanosoma cruzi epimastigotes were extracted under various conditions in order to examine the role of divalent cations in the solubilization of microtubule proteins. When epimastigotes were homogenized in the presence of 5 mM Mg+2 and 5 mM Ca+2, a protein kinase responsible for phosphorylating tubulin, as well as the tubulin that became phosphorylated, remained tightly associated with the parasite particulate and detergent-resistant fractions. On the contrary, tubulin kinase and its substrate were predominantly released into the parasite cytosolic and detergent-soluble fractions, when epimastigotes were extracted in the presence of 5 mM EDTA and 5 mM EGTA. These evidences demonstrated a divalent cation-dependent solubilization of the enzyme responsible...
Tipo: Journal article Palavras-chave: Microtubules; Post-translational modification of tubulin; Protein kinase CK2; Protein phosphorylation-dephosphorylation; Signal transduction; Trypanosoma cruzi; Tubulin.
Ano: 2003 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000300008
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