Influencing its molecular weight determination

En:

Int. J. Biochem. 1980;12(5-6):757-760

Fecha:

1980

Formato:

application/pdf

Tipo de documento:

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

Descriptores:

porphobilinogen synthase -  potassium -  animal -  article -  enzymology -  isolation and purification -  liver -  macromolecule -  metabolism

Descripción:

1. 1. By chromatography through Sephadex G-200 of increasing amounts of partially purified pig liver ALA-D, different profiles were obtained, showing that species of molecular weights ranging from 140,000 to 560,000 might exist in equilibrium, but their relative ratio was dependent on the total amount of protein sampled. In all cases, however, the main peak (60-70%) corresponded to the 280,000 MW oligomer, that is the octamer. 2. 2. It was found that elution profiles were also dependent on column dimensions and on the purity of the enzyme preparation. 3. 3. K+ ions affected both catalytic activity and aggregation of the enzyme. 4. Results here reported add further support to the proposal of the existence of a minimal functional dimer. © 1980.
Fil:Stella, A.M. 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_p757_Stafforini

Derechos:

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