Heme synthetase in Trypanosoma cruzi

1. 1. Heme-synthetase (Heme-S) has been studied in the epimastigote form of T. cruzi (Tulahuen and Y strains). 2. 2. The enzyme is confined to the "mitochondrial" fraction (sedimented at 30,000g). 3. 3. Activity was dependent on protein and time of cell storage. 4. 4. Enzymic proto- and me...

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Autores principales:	Salzman, Teresa Ana, Batlle, Alcira María del Carmen
Publicado:	1986
Materias:	divalent cation ferrochelatase iron lyase animal article cell fractionation enzymology kinetics metabolism mitochondrion Trypanosoma cruzi Animal Cations, Divalent Ferrochelatase Iron Kinetics Lyases Mitochondria Subcellular Fractions Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v85_n3_p537_Salzman http://hdl.handle.net/20.500.12110/paper_03050491_v85_n3_p537_Salzman
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_03050491_v85_n3_p537_Salzman
record_format	dspace
spelling	paper:paper_03050491_v85_n3_p537_Salzman2025-07-30T18:07:57Z Heme synthetase in Trypanosoma cruzi Salzman, Teresa Ana Batlle, Alcira María del Carmen divalent cation ferrochelatase iron lyase animal article cell fractionation enzymology kinetics metabolism mitochondrion Trypanosoma cruzi Animal Cations, Divalent Ferrochelatase Iron Kinetics Lyases Mitochondria Subcellular Fractions Support, Non-U.S. Gov't Trypanosoma cruzi 1. 1. Heme-synthetase (Heme-S) has been studied in the epimastigote form of T. cruzi (Tulahuen and Y strains). 2. 2. The enzyme is confined to the "mitochondrial" fraction (sedimented at 30,000g). 3. 3. Activity was dependent on protein and time of cell storage. 4. 4. Enzymic proto- and meso-heme formation was inhibited up to 40 and 72% respectively by Triton X-100. 5. 5. The optimum pH was 7.2 for protoheme and 7.5 for mesoheme formation. 6. 6. Heme-S reached its maximum when the concentration values were 37; 35 and 32 μM for proto-, meso-, and deuteroporphyrin, respectively. The activity is several times higher when mesoporphyrin is used as substrate. 7. 7. At a final cone of 100 μM Fe2+ and Zn2+ ions enhanced activity 200-400%. Cu2+ and Co2+ had no effect, while Mn2+ and Mg2+ were highly inhibitory. A combination of Fe2+ and Zn2+ at varying concentrations still showed great activation. However, at a fixed level of Fe2+, Cu2+ was changed into a strong inhibitor. 8. 8. We propose that, if it can be demonstrated that T. cruzi cannot multiply when protoheme is replaced by mesoheme, administration of mesoporphyrin would then greatly affect replication of T. cruzi. Furthermore, the addition of certain metals, such as Cu2+ to T. cruzi cultures might specifically inhibit the parasite enzyme opening the possibility of selectively destroying the hemoflagellate without affecting the host. © 1986. Fil:Salzman, T.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v85_n3_p537_Salzman http://hdl.handle.net/20.500.12110/paper_03050491_v85_n3_p537_Salzman
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	divalent cation ferrochelatase iron lyase animal article cell fractionation enzymology kinetics metabolism mitochondrion Trypanosoma cruzi Animal Cations, Divalent Ferrochelatase Iron Kinetics Lyases Mitochondria Subcellular Fractions Support, Non-U.S. Gov't Trypanosoma cruzi
spellingShingle	divalent cation ferrochelatase iron lyase animal article cell fractionation enzymology kinetics metabolism mitochondrion Trypanosoma cruzi Animal Cations, Divalent Ferrochelatase Iron Kinetics Lyases Mitochondria Subcellular Fractions Support, Non-U.S. Gov't Trypanosoma cruzi Salzman, Teresa Ana Batlle, Alcira María del Carmen Heme synthetase in Trypanosoma cruzi
topic_facet	divalent cation ferrochelatase iron lyase animal article cell fractionation enzymology kinetics metabolism mitochondrion Trypanosoma cruzi Animal Cations, Divalent Ferrochelatase Iron Kinetics Lyases Mitochondria Subcellular Fractions Support, Non-U.S. Gov't Trypanosoma cruzi
description	1. 1. Heme-synthetase (Heme-S) has been studied in the epimastigote form of T. cruzi (Tulahuen and Y strains). 2. 2. The enzyme is confined to the "mitochondrial" fraction (sedimented at 30,000g). 3. 3. Activity was dependent on protein and time of cell storage. 4. 4. Enzymic proto- and meso-heme formation was inhibited up to 40 and 72% respectively by Triton X-100. 5. 5. The optimum pH was 7.2 for protoheme and 7.5 for mesoheme formation. 6. 6. Heme-S reached its maximum when the concentration values were 37; 35 and 32 μM for proto-, meso-, and deuteroporphyrin, respectively. The activity is several times higher when mesoporphyrin is used as substrate. 7. 7. At a final cone of 100 μM Fe2+ and Zn2+ ions enhanced activity 200-400%. Cu2+ and Co2+ had no effect, while Mn2+ and Mg2+ were highly inhibitory. A combination of Fe2+ and Zn2+ at varying concentrations still showed great activation. However, at a fixed level of Fe2+, Cu2+ was changed into a strong inhibitor. 8. 8. We propose that, if it can be demonstrated that T. cruzi cannot multiply when protoheme is replaced by mesoheme, administration of mesoporphyrin would then greatly affect replication of T. cruzi. Furthermore, the addition of certain metals, such as Cu2+ to T. cruzi cultures might specifically inhibit the parasite enzyme opening the possibility of selectively destroying the hemoflagellate without affecting the host. © 1986.
author	Salzman, Teresa Ana Batlle, Alcira María del Carmen
author_facet	Salzman, Teresa Ana Batlle, Alcira María del Carmen
author_sort	Salzman, Teresa Ana
title	Heme synthetase in Trypanosoma cruzi
title_short	Heme synthetase in Trypanosoma cruzi
title_full	Heme synthetase in Trypanosoma cruzi
title_fullStr	Heme synthetase in Trypanosoma cruzi
title_full_unstemmed	Heme synthetase in Trypanosoma cruzi
title_sort	heme synthetase in trypanosoma cruzi
publishDate	1986
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v85_n3_p537_Salzman http://hdl.handle.net/20.500.12110/paper_03050491_v85_n3_p537_Salzman
work_keys_str_mv	AT salzmanteresaana hemesynthetaseintrypanosomacruzi AT batllealciramariadelcarmen hemesynthetaseintrypanosomacruzi
_version_	1840321431444914176

Heme synthetase in Trypanosoma cruzi

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