Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase

Trypanosoma cruzi epimastigote forms showed a tightly bound Ca2+-calmodulin-dependent protein kinase activity, which could be partially extracted from membranes and axonemes. The enzyme is constituted by subunits which were autophosphorylated in the absence of exogenous substrates. An antibody again...

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Autores principales: Ogueta, S.B., Solari, A., Téllez-Iñón, M.T.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00145793_v337_n3_p293_Ogueta
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spelling todo:paper_00145793_v337_n3_p293_Ogueta2023-10-03T14:13:03Z Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase Ogueta, S.B. Solari, A. Téllez-Iñón, M.T. Ca2+-calmodulin protein kinase Cytoskeleton Flagella Trypanosoma cruzi Trypanosomatid protein kinase (calcium,calmodulin) ii article cytoskeleton epimastigote flagellum nonhuman priority journal trypanosoma cruzi Animal Binding Sites Brain Ca(2+)-Calmodulin Dependent Protein Kinase Calmodulin Cattle Cell Fractionation Cell Membrane Comparative Study Cytoskeleton Flagella Microscopy, Electron Support, Non-U.S. Gov't Trypanosoma cruzi Trypanosoma cruzi epimastigote forms showed a tightly bound Ca2+-calmodulin-dependent protein kinase activity, which could be partially extracted from membranes and axonemes. The enzyme is constituted by subunits which were autophosphorylated in the absence of exogenous substrates. An antibody against CaM kinase II recognized a Ca2+- or Ca2+-CaM-dependent conformational epitope in these fractions. The detected bands were of molecular weights similar to the α and β subunits of the corresponding bovine brain enzyme (60 and 50 kDa). Studies using [125I]CaM revealed the presence of a CaM-binding domain. These experiments confirm that the parasite possesses a paniculate CaM kinase with characteristics similar to the bovine brain enzyme. © 1994. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00145793_v337_n3_p293_Ogueta
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Ca2+-calmodulin protein kinase
Cytoskeleton
Flagella
Trypanosoma cruzi
Trypanosomatid
protein kinase (calcium,calmodulin) ii
article
cytoskeleton
epimastigote
flagellum
nonhuman
priority journal
trypanosoma cruzi
Animal
Binding Sites
Brain
Ca(2+)-Calmodulin Dependent Protein Kinase
Calmodulin
Cattle
Cell Fractionation
Cell Membrane
Comparative Study
Cytoskeleton
Flagella
Microscopy, Electron
Support, Non-U.S. Gov't
Trypanosoma cruzi
spellingShingle Ca2+-calmodulin protein kinase
Cytoskeleton
Flagella
Trypanosoma cruzi
Trypanosomatid
protein kinase (calcium,calmodulin) ii
article
cytoskeleton
epimastigote
flagellum
nonhuman
priority journal
trypanosoma cruzi
Animal
Binding Sites
Brain
Ca(2+)-Calmodulin Dependent Protein Kinase
Calmodulin
Cattle
Cell Fractionation
Cell Membrane
Comparative Study
Cytoskeleton
Flagella
Microscopy, Electron
Support, Non-U.S. Gov't
Trypanosoma cruzi
Ogueta, S.B.
Solari, A.
Téllez-Iñón, M.T.
Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase
topic_facet Ca2+-calmodulin protein kinase
Cytoskeleton
Flagella
Trypanosoma cruzi
Trypanosomatid
protein kinase (calcium,calmodulin) ii
article
cytoskeleton
epimastigote
flagellum
nonhuman
priority journal
trypanosoma cruzi
Animal
Binding Sites
Brain
Ca(2+)-Calmodulin Dependent Protein Kinase
Calmodulin
Cattle
Cell Fractionation
Cell Membrane
Comparative Study
Cytoskeleton
Flagella
Microscopy, Electron
Support, Non-U.S. Gov't
Trypanosoma cruzi
description Trypanosoma cruzi epimastigote forms showed a tightly bound Ca2+-calmodulin-dependent protein kinase activity, which could be partially extracted from membranes and axonemes. The enzyme is constituted by subunits which were autophosphorylated in the absence of exogenous substrates. An antibody against CaM kinase II recognized a Ca2+- or Ca2+-CaM-dependent conformational epitope in these fractions. The detected bands were of molecular weights similar to the α and β subunits of the corresponding bovine brain enzyme (60 and 50 kDa). Studies using [125I]CaM revealed the presence of a CaM-binding domain. These experiments confirm that the parasite possesses a paniculate CaM kinase with characteristics similar to the bovine brain enzyme. © 1994.
format JOUR
author Ogueta, S.B.
Solari, A.
Téllez-Iñón, M.T.
author_facet Ogueta, S.B.
Solari, A.
Téllez-Iñón, M.T.
author_sort Ogueta, S.B.
title Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase
title_short Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase
title_full Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase
title_fullStr Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase
title_full_unstemmed Trypanosoma cruzi epimastigote forms possess a Ca2+-calmodulin dependent protein kinase
title_sort trypanosoma cruzi epimastigote forms possess a ca2+-calmodulin dependent protein kinase
url http://hdl.handle.net/20.500.12110/paper_00145793_v337_n3_p293_Ogueta
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