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

En:

Int. J. Biochem. 1980;12(5-6):721-724

Fecha:

1980

Formato:

application/pdf

Tipo de documento:

info:eu-repo/semantics/article
info:ar-repo/semantics/artículo
info:eu-repo/semantics/publishedVersion

Descriptores:

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

Descripción:

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.

Identificador(es):

http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p721_Vazquez

Derechos:

info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar