Heme synthesis in Crithidia deanei: Influence of the endosymbiote

• Autores: Salzman, T.A.; Del Batlle, C.A.M.; Angluster, J.; De Souza, W.
• Año de publicación: 1985
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: Int. J. Biochem. 1985;17(12):1343-1347
• Materia: 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
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

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.