Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase
1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM...
Guardado en:
Autor principal: | |
---|---|
Publicado: |
1991
|
Materias: | |
Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v98_n1_p67_Navone http://hdl.handle.net/20.500.12110/paper_03050491_v98_n1_p67_Navone |
Aporte de: |
id |
paper:paper_03050491_v98_n1_p67_Navone |
---|---|
record_format |
dspace |
spelling |
paper:paper_03050491_v98_n1_p67_Navone2023-06-08T15:30:25Z Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase Batlle, Alcira María del Carmen porphobilinogen deaminase porphobilinogenase unclassified drug uroporphyrinogen iii synthase animal tissue article breast adenocarcinoma liver male mouse nonhuman priority journal Ammonia-Lyases Animal Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Neoplasm Transplantation Porphyrins Support, Non-U.S. Gov't Temperature Animalia 1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM, Vmax of 1.57-1.83 nmol porphyrins/2 hr and a Hill coefficient of n = 1 were obtained for PBGase and Km values of 13 to 19 μM and Vmax of 2.6-4.8 were obtained for HMB-S. 3. 3. Porphyrin synthesis was linear up to 180 min of incubation in all cases for PBGase and HMB-S, and greatly increased with higher incubation temperature being maximal at 60°C and nil at 70°C, optimal temperature was 37°C for either enzyme in either source. 4. 4. Uroporphyrinogen III synthetase was heat inactivated while HMB-S was a heat stable enzyme. Optimum pH was 8.2 for PBGase and HMB-S in either tissue. © 1991. Fil:M. del C. Batlle, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1991 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v98_n1_p67_Navone http://hdl.handle.net/20.500.12110/paper_03050491_v98_n1_p67_Navone |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
porphobilinogen deaminase porphobilinogenase unclassified drug uroporphyrinogen iii synthase animal tissue article breast adenocarcinoma liver male mouse nonhuman priority journal Ammonia-Lyases Animal Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Neoplasm Transplantation Porphyrins Support, Non-U.S. Gov't Temperature Animalia |
spellingShingle |
porphobilinogen deaminase porphobilinogenase unclassified drug uroporphyrinogen iii synthase animal tissue article breast adenocarcinoma liver male mouse nonhuman priority journal Ammonia-Lyases Animal Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Neoplasm Transplantation Porphyrins Support, Non-U.S. Gov't Temperature Animalia Batlle, Alcira María del Carmen Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
topic_facet |
porphobilinogen deaminase porphobilinogenase unclassified drug uroporphyrinogen iii synthase animal tissue article breast adenocarcinoma liver male mouse nonhuman priority journal Ammonia-Lyases Animal Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Neoplasm Transplantation Porphyrins Support, Non-U.S. Gov't Temperature Animalia |
description |
1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM, Vmax of 1.57-1.83 nmol porphyrins/2 hr and a Hill coefficient of n = 1 were obtained for PBGase and Km values of 13 to 19 μM and Vmax of 2.6-4.8 were obtained for HMB-S. 3. 3. Porphyrin synthesis was linear up to 180 min of incubation in all cases for PBGase and HMB-S, and greatly increased with higher incubation temperature being maximal at 60°C and nil at 70°C, optimal temperature was 37°C for either enzyme in either source. 4. 4. Uroporphyrinogen III synthetase was heat inactivated while HMB-S was a heat stable enzyme. Optimum pH was 8.2 for PBGase and HMB-S in either tissue. © 1991. |
author |
Batlle, Alcira María del Carmen |
author_facet |
Batlle, Alcira María del Carmen |
author_sort |
Batlle, Alcira María del Carmen |
title |
Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
title_short |
Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
title_full |
Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
title_fullStr |
Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
title_full_unstemmed |
Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
title_sort |
mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase |
publishDate |
1991 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v98_n1_p67_Navone http://hdl.handle.net/20.500.12110/paper_03050491_v98_n1_p67_Navone |
work_keys_str_mv |
AT batllealciramariadelcarmen mousemammarycarcinomaporphobilinogenaseandhydroxymethylbilanesynthetase |
_version_ |
1768543084172279808 |