Porphyrin biosynthesis in the soybean callus tissue system-XVIII. Levels of succinyl coa synthetase, cysthationase, rhodanese, aminolevulinate synthetase and aminolevulinate dehydr...

• Autores: Vazquez, E.; De Xifra, E.W.; Del C. Batlle, A.M.
• Año de publicación: 1980
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: Int. J. Biochem. 1980;12(5-6):721-724
• Materia: 5 aminolevulinate synthase; cystathionine gamma lyase; long chain fatty acid coenzyme A ligase; lyase; porphobilinogen synthase; porphyrin; Succinate CoA Ligases; succinyl coenzyme A synthetase; sulfurtransferase; thiosulfate sulfurtransferase; article; biosynthesis; cell clone; cell culture; enzymology; growth, development and aging; metabolism; plant; soybean; 5-Aminolevulinate Synthetase; Cells, Cultured; Clone Cells; Coenzyme A Ligases; Cystathionine gamma-Lyase; Lyases; Plants; Porphobilinogen Synthase; Porphyrins; Soybeans; Succinate-CoA Ligases; Sulfurtransferases; Support, Non-U.S. Gov't; Thiosulfate Sulfurtransferase
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

1. 1. The activity of Succinyl CoA Synthetase (Suc CoA-S), Cysthationase, Rhodanese, Aminolevulinate Synthetase (ALA-S) and Aminolevulinate Dehydratase (ALA-D) was studied in old (405-407 subcultures) and young (34-36 subcultures) soybean callus clones as a function of the days of growing. 2. 2. Suc CoA-S, ALA-S and ALA-D activities were much lower in old than in young callus, while the activity of Cysthationase and Rhodanese was higher in old callus. 3. 3. ALA-S reached its maximum activity when Rhodanese and Cysthationase their minimum, on the 11th day of growth. It is suggested that the cellular content of a possible thio-compound which would regulate ALA-S activity, is controlled through its degradation by Rhodanese. © 1980.
Fil:Vazquez, E. 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.