Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties

Several properties of porphyrinogen carboxy-lyase from normal chicken erythrocytes were studied. 1. 1. The utilization of the substrate uroporphyrinogen (8-COOH), and the formation of intermediate products (porphyrinogens of 7-, 6- and 5-COOH) and the final product coproporphyrinogen (4-COOH) were i...

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Autores principales: Garcia, R.C., San Martin de Viale, L.C., Tomio, J.M., Grinstein, M.
Formato: JOUR
Materias:
carboxylase
coproporphyrinogen
porphyrin
uroporphyrinogen
uroporphyrinogen decarboxylase
erythrocyte
theoretical study
Anaerobiosis
Animal
Carboxy-Lyases
Chickens
Chromatography, DEAE-Cellulose
Cysteine
Darkness
Erythrocytes
Glutathione
Kinetics
Porphyrins
Rats
Sulfhydryl Compounds
Temperature
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v309_n1_p203_Garcia
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_00052744_v309_n1_p203_Garcia2023-10-03T14:03:29Z Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties Garcia, R.C. San Martin de Viale, L.C. Tomio, J.M. Grinstein, M. carboxylase coproporphyrinogen porphyrin uroporphyrinogen uroporphyrinogen decarboxylase erythrocyte theoretical study Anaerobiosis Animal Carboxy-Lyases Chickens Chromatography, DEAE-Cellulose Cysteine Darkness Erythrocytes Glutathione Kinetics Porphyrins Rats Sulfhydryl Compounds Temperature Several properties of porphyrinogen carboxy-lyase from normal chicken erythrocytes were studied. 1. 1. The utilization of the substrate uroporphyrinogen (8-COOH), and the formation of intermediate products (porphyrinogens of 7-, 6- and 5-COOH) and the final product coproporphyrinogen (4-COOH) were investigated as function of time and substrate concentration. The results confirm a two-stage hypothesis involving firstly, the elimination of the first carboxyl group from uroporphyrinogen and secondly the elimination of the further three carboxyl groups to form coproporphyrinogen. The elimination of the first carboxyl group is not the rate-limiting step in this multiple decarboxylation because large amounts of 7 COOH porphyrinogen were accumulated. The effect of temperature on the stepwise decarboxylation process also suggests and easier elimination of the first carboxyl group. 2. 2. Cysteine and glutathione inhibited the decarboxylation process at low concentrations, but at higher concentrations cysteine continues to inhibit while glutathione allows the recovery of enzyme activity. 3. 3. Studies of the effect of uroporphyrinogen concentration on the first and second stages; and of 7-COOH porphyrinogen concentration on the second stage revealed both substrates as inhibitors of their own decarboxylations. Furthermore, when 7-COOH porphyrinogen was incubated in the presence of uroporphyrinogen, it further inhibited the first decarboxylation of uroporphyrinogen, 7-COOH porphyrinogen was a stronger inhibitor than 8 COOH porphyrinogen. © 1973. Fil:Garcia, R.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:San Martin de Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Tomio, J.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00052744_v309_n1_p203_Garcia
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic carboxylase
coproporphyrinogen
porphyrin
uroporphyrinogen
uroporphyrinogen decarboxylase
erythrocyte
theoretical study
Anaerobiosis
Animal
Carboxy-Lyases
Chickens
Chromatography, DEAE-Cellulose
Cysteine
Darkness
Erythrocytes
Glutathione
Kinetics
Porphyrins
Rats
Sulfhydryl Compounds
Temperature
spellingShingle carboxylase
coproporphyrinogen
porphyrin
uroporphyrinogen
uroporphyrinogen decarboxylase
erythrocyte
theoretical study
Anaerobiosis
Animal
Carboxy-Lyases
Chickens
Chromatography, DEAE-Cellulose
Cysteine
Darkness
Erythrocytes
Glutathione
Kinetics
Porphyrins
Rats
Sulfhydryl Compounds
Temperature
Garcia, R.C.
San Martin de Viale, L.C.
Tomio, J.M.
Grinstein, M.
Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
topic_facet carboxylase
coproporphyrinogen
porphyrin
uroporphyrinogen
uroporphyrinogen decarboxylase
erythrocyte
theoretical study
Anaerobiosis
Animal
Carboxy-Lyases
Chickens
Chromatography, DEAE-Cellulose
Cysteine
Darkness
Erythrocytes
Glutathione
Kinetics
Porphyrins
Rats
Sulfhydryl Compounds
Temperature
description Several properties of porphyrinogen carboxy-lyase from normal chicken erythrocytes were studied. 1. 1. The utilization of the substrate uroporphyrinogen (8-COOH), and the formation of intermediate products (porphyrinogens of 7-, 6- and 5-COOH) and the final product coproporphyrinogen (4-COOH) were investigated as function of time and substrate concentration. The results confirm a two-stage hypothesis involving firstly, the elimination of the first carboxyl group from uroporphyrinogen and secondly the elimination of the further three carboxyl groups to form coproporphyrinogen. The elimination of the first carboxyl group is not the rate-limiting step in this multiple decarboxylation because large amounts of 7 COOH porphyrinogen were accumulated. The effect of temperature on the stepwise decarboxylation process also suggests and easier elimination of the first carboxyl group. 2. 2. Cysteine and glutathione inhibited the decarboxylation process at low concentrations, but at higher concentrations cysteine continues to inhibit while glutathione allows the recovery of enzyme activity. 3. 3. Studies of the effect of uroporphyrinogen concentration on the first and second stages; and of 7-COOH porphyrinogen concentration on the second stage revealed both substrates as inhibitors of their own decarboxylations. Furthermore, when 7-COOH porphyrinogen was incubated in the presence of uroporphyrinogen, it further inhibited the first decarboxylation of uroporphyrinogen, 7-COOH porphyrinogen was a stronger inhibitor than 8 COOH porphyrinogen. © 1973.
format JOUR
author Garcia, R.C.
San Martin de Viale, L.C.
Tomio, J.M.
Grinstein, M.
author_facet Garcia, R.C.
San Martin de Viale, L.C.
Tomio, J.M.
Grinstein, M.
author_sort Garcia, R.C.
title Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
title_short Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
title_full Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
title_fullStr Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
title_full_unstemmed Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
title_sort porphyrin biosynthesis. x. porphyrinogen carboxy-lyase from avian erythrocytes futher properties
url http://hdl.handle.net/20.500.12110/paper_00052744_v309_n1_p203_Garcia
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AT sanmartindevialelc porphyrinbiosynthesisxporphyrinogencarboxylyasefromavianerythrocytesfutherproperties
AT tomiojm porphyrinbiosynthesisxporphyrinogencarboxylyasefromavianerythrocytesfutherproperties
AT grinsteinm porphyrinbiosynthesisxporphyrinogencarboxylyasefromavianerythrocytesfutherproperties
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