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...
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todo:paper_03050491_v98_n1_p67_Navone2023-10-03T15:21:23Z Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase Navone, N.M. Polo, C.F. Frisardi, A.L. M. del C. Batlle, A. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Navone, N.M. Polo, C.F. Frisardi, A.L. M. del C. Batlle, A. 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. |
format |
JOUR |
author |
Navone, N.M. Polo, C.F. Frisardi, A.L. M. del C. Batlle, A. |
author_facet |
Navone, N.M. Polo, C.F. Frisardi, A.L. M. del C. Batlle, A. |
author_sort |
Navone, N.M. |
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 |
url |
http://hdl.handle.net/20.500.12110/paper_03050491_v98_n1_p67_Navone |
work_keys_str_mv |
AT navonenm mousemammarycarcinomaporphobilinogenaseandhydroxymethylbilanesynthetase AT polocf mousemammarycarcinomaporphobilinogenaseandhydroxymethylbilanesynthetase AT frisardial mousemammarycarcinomaporphobilinogenaseandhydroxymethylbilanesynthetase AT mdelcbatllea mousemammarycarcinomaporphobilinogenaseandhydroxymethylbilanesynthetase |
_version_ |
1807315272011350016 |