Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties

En:

BBA - Enzymology 1970;198(2):353-363

Fecha:

1970

Formato:

application/pdf

Tipo de documento:

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

Descriptores:

acrylic acid derivative -  ammonium derivative -  Carboxy Lyases -  carboxylyase -  cellulose -  edetic acid -  glutathione -  porphyrin -  sodium

Descripción:

1. 1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. 2. 2. The purified material appears to be homogeneous in polyacrylamide gel disc electrophoresis. 3. 3. The enzyme was heat labile and inhibited by sodium salt; the activity was enhanced by EDTA, GSH and boiled rat-liver extract. 4. 4. The influence of these chemical and physical agents on the removal of the first and second carboxyl groups from uroporphyrinogen was compared; the second group was more susceptible to these agents. 5. 5. The possibility that one or several enzymes were involved in the stepwise decarboxylation of uroporphyrinogen is discussed. 6. 6. The general name of porphyrinogen carboxy-lyase for the enzyme system is proposed because of the different porphyrinogens it can decarboxylate. © 1970.
Fil:Tomio, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:García, R.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:San Martín De Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.

Identificador(es):

http://hdl.handle.net/20.500.12110/paper_00052744_v198_n2_p353_Tomio

Derechos:

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