Cyclic AMP-dependent protein kinase activity in Trypanosoma cruzi

A cyclic AMP-dependent protein kinase activity from epimastigote forms of Trypanosoma cruzi was characterized. Cytosolic extracts were chromatographed on DEAE-cellulose columns, giving two peaks of kinase activity, which were eluted at 0.15 M- and 0.32 M-NaCl respectively. The second activity peak w...

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Autor principal: Ulloa, R.M
Otros Autores: Mesri, E., Esteva, M., Torres, H.N, Tellez-Inon, M.T
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1988
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 scopus  |a 2-s2.0-0023764268 
024 7 |2 cas  |a cyclic AMP, 60-92-4; protein kinase, 9026-43-1; Cyclic AMP, 60-92-4; Phosphates; Protein Kinases, EC 2.7.1.37 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BIJOA 
100 1 |a Ulloa, R.M. 
245 1 0 |a Cyclic AMP-dependent protein kinase activity in Trypanosoma cruzi 
260 |c 1988 
506 |2 openaire  |e Política editorial 
520 3 |a A cyclic AMP-dependent protein kinase activity from epimastigote forms of Trypanosoma cruzi was characterized. Cytosolic extracts were chromatographed on DEAE-cellulose columns, giving two peaks of kinase activity, which were eluted at 0.15 M- and 0.32 M-NaCl respectively. The second activity peak was stimulated by nanomolar concentrations of cyclic AMP. In addition, a cyclic AMP-binding protein co-eluted with the second kinase activity peak. Cyclic AMP-dependent protein kinase activity was further purified by gel filtration, affinity chromatography on histone-agarose and cyclic AMP-agarose, as well as by chromatography on CM-Sephadex. The enzyme ('holoenzyme') could be partially dissociated into two different components: 'catalytic' and 'regulatory'. The 'regulatory' component had specific binding for cyclic AMP, and it inhibited phosphotransferase activity of the homologous 'catalytic component' or of the 'catalytic subunit' from bovine heart. Cyclic AMP reversed these inhibitions. A 'holoenzyme preparation' was phosphorylated in the absence of exogenous phosphate acceptor and analyzed by polyacrylamide- gel electrophoresis. A 56 kDa band was phosphorylated. The same preparation was analysed by Western blotting, by using polyclonal antibodies to the regulatory subunits of protein kinases type I or II. Both antibodies reacted with the 56 kDa band.  |l eng 
593 |a Instituto de Investigaciones en Ingenieria Genetica y Biologia Molecular, 1428 Buenos Aires, Argentina 
690 1 0 |a ANTIBODY 
690 1 0 |a CYCLIC AMP 
690 1 0 |a PROTEIN KINASE 
690 1 0 |a IMMUNOBLOTTING 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTOZOON 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a ANIMAL 
690 1 0 |a CATTLE 
690 1 0 |a CHROMATOGRAPHY, AFFINITY 
690 1 0 |a CHROMATOGRAPHY, DEAE-CELLULOSE 
690 1 0 |a CHROMATOGRAPHY, GEL 
690 1 0 |a CYCLIC AMP 
690 1 0 |a IMMUNOBLOTTING 
690 1 0 |a MYOCARDIUM 
690 1 0 |a PHOSPHATES 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN KINASES 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
690 1 0 |a TRYPANOSOMA CRUZI 
700 1 |a Mesri, E. 
700 1 |a Esteva, M. 
700 1 |a Torres, H.N. 
700 1 |a Tellez-Inon, M.T. 
773 0 |d 1988  |g v. 255  |h pp. 319-326  |k n. 1  |p BIOCHEM. J.  |x 02646021  |w (AR-BaUEN)CENRE-205  |t Biochemical Journal 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_02646021_v255_n1_p319_Ulloa  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v255_n1_p319_Ulloa  |y Registro en la Biblioteca Digital 
961 |a paper_02646021_v255_n1_p319_Ulloa  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
963 |a VARI 
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