Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse
1. 1. URO-D was investigated in crude extracts from mouse mammary carcinoma, normal mouse (NM) liver and tumor-bearing mouse (TBM) liver. 2. 2. URO-D from TBM liver and tumor appears to be more sensitive to increasing concentrations of UROgen than the NM liver enzyme. 3. 3. In tumor the rate-limitin...
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todo:paper_03050491_v102_n1_p87_Navone2023-10-03T15:21:13Z Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse Navone, N.M. Afonso, S.G. Polo, C.F. del C. Battle, A.M. uroporphyrinogen decarboxylase animal tissue article breast cancer liver mouse nonhuman ph priority journal Animal Hydrogen-Ion Concentration Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Substrate Specificity Support, Non-U.S. Gov't Temperature Uroporphyrinogen Decarboxylase Uroporphyrinogens Animalia 1. 1. URO-D was investigated in crude extracts from mouse mammary carcinoma, normal mouse (NM) liver and tumor-bearing mouse (TBM) liver. 2. 2. URO-D from TBM liver and tumor appears to be more sensitive to increasing concentrations of UROgen than the NM liver enzyme. 3. 3. In tumor the rate-limiting step seems to be the decarboxylation of the first carboxyl group, but this was not so clear for the NM and the TBM liver URO-D. 4. 4. URO-D activity was enhanced when incubated at higher temperatures in the presence of its substrate, suggesting that UROgen might afford some protection of the enzyme against heat inactivation. 5. 5. The optimum pH for all three sources is around 7.0. © 1992. Fil:Afonso, S.G. 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_v102_n1_p87_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 |
uroporphyrinogen decarboxylase animal tissue article breast cancer liver mouse nonhuman ph priority journal Animal Hydrogen-Ion Concentration Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Substrate Specificity Support, Non-U.S. Gov't Temperature Uroporphyrinogen Decarboxylase Uroporphyrinogens Animalia |
| spellingShingle |
uroporphyrinogen decarboxylase animal tissue article breast cancer liver mouse nonhuman ph priority journal Animal Hydrogen-Ion Concentration Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Substrate Specificity Support, Non-U.S. Gov't Temperature Uroporphyrinogen Decarboxylase Uroporphyrinogens Animalia Navone, N.M. Afonso, S.G. Polo, C.F. del C. Battle, A.M. Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| topic_facet |
uroporphyrinogen decarboxylase animal tissue article breast cancer liver mouse nonhuman ph priority journal Animal Hydrogen-Ion Concentration Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Substrate Specificity Support, Non-U.S. Gov't Temperature Uroporphyrinogen Decarboxylase Uroporphyrinogens Animalia |
| description |
1. 1. URO-D was investigated in crude extracts from mouse mammary carcinoma, normal mouse (NM) liver and tumor-bearing mouse (TBM) liver. 2. 2. URO-D from TBM liver and tumor appears to be more sensitive to increasing concentrations of UROgen than the NM liver enzyme. 3. 3. In tumor the rate-limiting step seems to be the decarboxylation of the first carboxyl group, but this was not so clear for the NM and the TBM liver URO-D. 4. 4. URO-D activity was enhanced when incubated at higher temperatures in the presence of its substrate, suggesting that UROgen might afford some protection of the enzyme against heat inactivation. 5. 5. The optimum pH for all three sources is around 7.0. © 1992. |
| format |
JOUR |
| author |
Navone, N.M. Afonso, S.G. Polo, C.F. del C. Battle, A.M. |
| author_facet |
Navone, N.M. Afonso, S.G. Polo, C.F. del C. Battle, A.M. |
| author_sort |
Navone, N.M. |
| title |
Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| title_short |
Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| title_full |
Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| title_fullStr |
Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| title_full_unstemmed |
Uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| title_sort |
uroporhyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse |
| url |
http://hdl.handle.net/20.500.12110/paper_03050491_v102_n1_p87_Navone |
| work_keys_str_mv |
AT navonenm uroporhyrinogendecarboxylasefrommousemammarycarcinomaandliverofnormalandtumorbearingmouse AT afonsosg uroporhyrinogendecarboxylasefrommousemammarycarcinomaandliverofnormalandtumorbearingmouse AT polocf uroporhyrinogendecarboxylasefrommousemammarycarcinomaandliverofnormalandtumorbearingmouse AT delcbattleam uroporhyrinogendecarboxylasefrommousemammarycarcinomaandliverofnormalandtumorbearingmouse |
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