Heme synthesis in Crithidia deanei: Influence of the endosymbiote

1. 1. The activity of the following enzymes involved in the biosynthesis of porphyrins was determined in endosymbiote-free and endosymbiote-containing Crithidia deanei grown in a chemically defined medium: succinyl Coenzyme A synthetase (Suc.CoA-S), 5-aminolevulinate synthetase (ALA-S), 4,5-dioxoval...

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Autores principales:	Salzman, Teresa Ana, Batlle, Alcira María del Carmen
Publicado:	1985
Materias:	enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v17_n12_p1343_Salzman http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_Salzman
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_0020711X_v17_n12_p1343_Salzman
record_format	dspace
spelling	paper:paper_0020711X_v17_n12_p1343_Salzman2023-06-08T14:41:06Z Heme synthesis in Crithidia deanei: Influence of the endosymbiote Salzman, Teresa Ana Batlle, Alcira María del Carmen enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis 1. 1. The activity of the following enzymes involved in the biosynthesis of porphyrins was determined in endosymbiote-free and endosymbiote-containing Crithidia deanei grown in a chemically defined medium: succinyl Coenzyme A synthetase (Suc.CoA-S), 5-aminolevulinate synthetase (ALA-S), 4,5-dioxovaleric acid transaminase (DOVA-T), 5-aminolevulinate dehydratase (ALA-D), por- phobilinogenase (PBGase), deaminase and heme synthetase (Heme-S). The amount of 5-aminolevulinic acid (ALA) and porphobilinogen, porphyrins and heme was also determined. 2. 2. ALA and PBG were detected in C. deanei. The levels of free porphyrins was low. Heme concentration was nil. 3. 3. The activity of ALA-D. deaminase and PBGase was not detected in C deanei. 4. 4. The activity of Suc.CoA-S and ALA-S were twice higher in symbiote-containing than in aposymbiotic C. deanei. Aposymbiotic cells had a higher activity of DOVA-T than symbiote-containing cells. 5. 5. The level of Heme-S, measured using protoporphyrin as substrate, was twice as high in symbiotecontaining than in symbiote-free cells,. © 1985. Fil:Salzman, T.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del Batlle, C.A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1985 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v17_n12_p1343_Salzman http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_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	enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis
spellingShingle	enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis Salzman, Teresa Ana Batlle, Alcira María del Carmen Heme synthesis in Crithidia deanei: Influence of the endosymbiote
topic_facet	enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis
description	1. 1. The activity of the following enzymes involved in the biosynthesis of porphyrins was determined in endosymbiote-free and endosymbiote-containing Crithidia deanei grown in a chemically defined medium: succinyl Coenzyme A synthetase (Suc.CoA-S), 5-aminolevulinate synthetase (ALA-S), 4,5-dioxovaleric acid transaminase (DOVA-T), 5-aminolevulinate dehydratase (ALA-D), por- phobilinogenase (PBGase), deaminase and heme synthetase (Heme-S). The amount of 5-aminolevulinic acid (ALA) and porphobilinogen, porphyrins and heme was also determined. 2. 2. ALA and PBG were detected in C. deanei. The levels of free porphyrins was low. Heme concentration was nil. 3. 3. The activity of ALA-D. deaminase and PBGase was not detected in C deanei. 4. 4. The activity of Suc.CoA-S and ALA-S were twice higher in symbiote-containing than in aposymbiotic C. deanei. Aposymbiotic cells had a higher activity of DOVA-T than symbiote-containing cells. 5. 5. The level of Heme-S, measured using protoporphyrin as substrate, was twice as high in symbiotecontaining than in symbiote-free cells,. © 1985.
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 synthesis in Crithidia deanei: Influence of the endosymbiote
title_short	Heme synthesis in Crithidia deanei: Influence of the endosymbiote
title_full	Heme synthesis in Crithidia deanei: Influence of the endosymbiote
title_fullStr	Heme synthesis in Crithidia deanei: Influence of the endosymbiote
title_full_unstemmed	Heme synthesis in Crithidia deanei: Influence of the endosymbiote
title_sort	heme synthesis in crithidia deanei: influence of the endosymbiote
publishDate	1985
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v17_n12_p1343_Salzman http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_Salzman
work_keys_str_mv	AT salzmanteresaana hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote AT batllealciramariadelcarmen hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote
_version_	1768545863004585984

Heme synthesis in Crithidia deanei: Influence of the endosymbiote

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