Heme synthesis in Crithidia deanei: Influence of the endosymbiote

Mostrar todas las versiones(3)

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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Salzman, T.A., Del Batlle, C.A.M., Angluster, J., De Souza, W.
Formato: JOUR
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: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 todo:paper_0020711X_v17_n12_p1343_Salzman
record_format dspace
spelling todo:paper_0020711X_v17_n12_p1343_Salzman2023-10-03T14:17:48Z Heme synthesis in Crithidia deanei: Influence of the endosymbiote Salzman, T.A. Del Batlle, C.A.M. Angluster, J. De Souza, W. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, T.A.
Del Batlle, C.A.M.
Angluster, J.
De Souza, W.
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.
format JOUR
author Salzman, T.A.
Del Batlle, C.A.M.
Angluster, J.
De Souza, W.
author_facet Salzman, T.A.
Del Batlle, C.A.M.
Angluster, J.
De Souza, W.
author_sort Salzman, T.A.
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
url http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_Salzman
work_keys_str_mv AT salzmanta hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote
AT delbatllecam hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote
AT anglusterj hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote
AT desouzaw hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote
_version_ 1807316123488616448

Ejemplares similares