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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Autor principal: Salzman, T.A
Otros Autores: del C. Batlle, A.M
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1986
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0022961774 
024 7 |2 cas  |a ferrochelatase, 9012-93-5; iron, 14093-02-8, 53858-86-9, 7439-89-6; lyase, 9055-04-3; Cations, Divalent; Ferrochelatase, EC 4.99.1.1; Iron, 7439-89-6; Lyases, EC 4. 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
100 1 |a Salzman, T.A. 
245 1 0 |a Heme synthetase in Trypanosoma cruzi 
260 |c 1986 
270 1 0 |m del C. Batlle, A.M.; Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP, (CONICET-FCEN, UBA), Ciudad Universitaria, Pab. II, 1428 Nuñez Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Chang, Sassa, Heme biosynthesis in bacterium-protozoon symbiosis: enzymic defects in host hemoflagellates and complemental role of their intracellular symbiotes (1975) Proc. natn. Acad. Sci., U.S.A., 72, pp. 2979-2983 
504 |a Docampo, de, Stoppani, Tricarboxylic acid cycle operation at the kinetoplastmitochondrion complex of Trypanosoma cruzi (1978) Biochim. Biophys. Acta, 502, pp. 466-476 
504 |a Gaugham, Krassner, Hemin deprivation in culture stages of hemoflagellates Leishmania tarentolae (1971) Comp. Biochem. Physiol., 39 B, pp. 5-18 
504 |a Hutner, Bacchi, Baker, Nutrition of the kinetoplastida (1979) Biology of the kinetoplastida, pp. 654-691. , W.H.R. Lumsden, D.A. Evans, Academic Press, New York, N°2 
504 |a Jensen, Thofern, Clhoramin (ferroporphyrin chloride) als bakterienurichsstoff (1953) Naturforshung, 86, pp. 599-607 
504 |a Johnson, Jones, Enzymic formation of haems and other metalloporphyrins (1964) Biochim. Biophys. Acta, 93, pp. 171-173 
504 |a Lochhead, Goldberg, The enzymic formation of haem by human and rat tissues (1961) Biochem. J., 78, pp. 146-150 
504 |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275 
504 |a Lwoff, The nutrition of parasitic flagellates (Trypanosomidae, Trichomonadinae) (1951) Biochemistry and Physiology of Protazoa, pp. 131-182. , A. Lwoff, Academic Press, New York 
504 |a Porra, Jones, Studies on ferrochelatase I. Assay and properties of ferrochelatase from a pig liver mitochondrial extract (1963) Biochem. J., 87, pp. 181-185 
504 |a Porra, Jones, An investigation of the role of ferrochelatase in the biosynthesis of various haem groups (1963) Biochem. J., 87, pp. 186-192 
504 |a Salzman, Batlle, Angluster, De Souza, Heme synthesis in Crithidia deanei: influence of the endosymbiote (1985) Int. J. Biochem., 17, pp. 1343-1347 
504 |a Salzman, Batlle, De Souza, Heme synthesis in Trypanosoma cruzi: influence of the strain and culture medium (1986) Comp. Biochem. Physiol., 86 B, pp. 57-61 
504 |a Salzman, Stella, Wider de Xifra, Batlle, Docampo, Stoppani, Porphyrin biosynthesis in parasitic hemoflagellates functional and defective enzymes in Trypanosoma cruzi (1982) Comp. Biochem. Physiol., 72 B, pp. 663-667 
504 |a Simpson, Poulson, Effects of lipids on the activity of ferrochelatase (1977) Biochim. biophys. Acta, 482 (2), pp. 461-469 
504 |a Taketani, Tokunaga, Rat liver ferrochelatase (1981) Purification, properties and stimulation by fatty acids, 256, pp. 12748-12753. , J. biol. Chem 
504 |a Tokunaga, Sano, Comparative studies of non-enzymic and enzymic protoheme formation (1972) Biochim. biophys. Acta, 264, pp. 263-271 
504 |a Ulvik, Romslo, Studies on the utilization of ferritin iron in the ferrochelatase reaction of isolated rat liver mitochondria (1978) Biochim. biophys. Acta, 541, pp. 251-262 
504 |a Warren, Metabolism of Schizotrypanum cruzi Chagas I. Effect of culture age and substrate concentration on respiratory rate (1960) J. Parasit., 46, pp. 529-539 
520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: Secretaria de Ciencia y Tecnica, Universidad de Buenos Aires 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Acknowledgements--This work was supported by grants from the Consejo Nacional de Investigaciones Cientificas y T6nicas (CONICET), B. Aires, Argentine, The SECYT, Banco de la Naci6n Argentina, Min. de Salud Pfiblica. A. M. del C. Batlle holds the post of Principal Scientific Researcher in the CONICET. This work forms part of the Thesis of T. A. Salzman to be submitted to the University of Buenos Aires for her Ph.D. degree. We are very grateful to Dr Roberto Docampo and Prof. Andr6s O. M. Stoppani from the CIBIERG (CONICET and FCM-UBA) for their most valuable support throughout this work and providing us with the Tulahuen strain of T. cruzi; also to Dr Ana SteUa and Eva Wider for their help in the performance of some preliminary experiments. We extend our thanks to Dr Wanderley De Souza (Instituto de Biofisica-UFRJ, R. J., Brasil) for generously giving us the Y strain of 7". cruzi. The technical assistance of Mrs B. Riccillo is also acknowledged. Finally we also wish to express our gratitude to Arquitect Hugo E. Salzman for the excellent drawings and to Miss Claudia Tedesco for help with the final typing. 
593 |a Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP, (CONICET-FCEN, UBA), Ciudad Universitaria, Pab. II, 1428 Nuñez Buenos Aires, Argentina 
690 1 0 |a DIVALENT CATION 
690 1 0 |a FERROCHELATASE 
690 1 0 |a IRON 
690 1 0 |a LYASE 
690 1 0 |a ANIMAL 
690 1 0 |a ARTICLE 
690 1 0 |a CELL FRACTIONATION 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a KINETICS 
690 1 0 |a METABOLISM 
690 1 0 |a MITOCHONDRION 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a ANIMAL 
690 1 0 |a CATIONS, DIVALENT 
690 1 0 |a FERROCHELATASE 
690 1 0 |a IRON 
690 1 0 |a KINETICS 
690 1 0 |a LYASES 
690 1 0 |a MITOCHONDRIA 
690 1 0 |a SUBCELLULAR FRACTIONS 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
690 1 0 |a TRYPANOSOMA CRUZI 
700 1 |a del C. Batlle, A.M. 
773 0 |d 1986  |g v. 85  |h pp. 537-541  |k n. 3  |x 03050491  |w (AR-BaUEN)CENRE-2752  |t Comparative Biochemistry and Physiology -- Part B: Biochemistry and 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_03050491_v85_n3_p537_Salzman  |y Handle 
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