Mouse mammary carcinoma δ-aminolevulinate dehydratase

1. 1. Aminolevulinate dehydratase (ALA-D) was studied in crude extract from mouse mammary carcinoma, normal mouse liver and tumour bearing mouse liver. 2. 2. A Michaelis-Menten behaviour and Km values between 0.24 and 0.31 mM were obtained for the enzyme in either source. 3. 3. In all three tissues...

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Autores principales: Navone, N.M., Polo, C.F., Frisardi, A.L., Batlle, A.M.D.C.
Formato: JOUR
Materias:
liver enzyme
porphobilinogen synthase
animal cell
article
breast cancer
enzyme kinetics
mouse
nonhuman
priority journal
Animal
Enzyme Stability
Heat
Hydrogen-Ion Concentration
Kinetics
Liver
Male
Mammary Neoplasms, Experimental
Mice
Mice, Inbred BALB C
Porphobilinogen
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Animalia
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03050491_v96_n4_p729_Navone
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_03050491_v96_n4_p729_Navone
record_format dspace
spelling todo:paper_03050491_v96_n4_p729_Navone2023-10-03T15:21:23Z Mouse mammary carcinoma δ-aminolevulinate dehydratase Navone, N.M. Polo, C.F. Frisardi, A.L. Batlle, A.M.D.C. liver enzyme porphobilinogen synthase animal cell article breast cancer enzyme kinetics mouse nonhuman priority journal Animal Enzyme Stability Heat Hydrogen-Ion Concentration Kinetics Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Porphobilinogen Porphobilinogen Synthase Support, Non-U.S. Gov't Animalia 1. 1. Aminolevulinate dehydratase (ALA-D) was studied in crude extract from mouse mammary carcinoma, normal mouse liver and tumour bearing mouse liver. 2. 2. A Michaelis-Menten behaviour and Km values between 0.24 and 0.31 mM were obtained for the enzyme in either source. 3. 3. In all three tissues there was a linear relationship between porphobilinogen formation and incubation time, up to 120 min, ALA-D was thermostable and optimum pH was at 6.8. 4. 4. There seems to be no structural alterations in tumoural ALA-D as compared with the enzyme from liver of both normal and tumour bearing mice. © 1990. Fil:Batlle, A.M.D.C. 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_v96_n4_p729_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 liver enzyme
porphobilinogen synthase
animal cell
article
breast cancer
enzyme kinetics
mouse
nonhuman
priority journal
Animal
Enzyme Stability
Heat
Hydrogen-Ion Concentration
Kinetics
Liver
Male
Mammary Neoplasms, Experimental
Mice
Mice, Inbred BALB C
Porphobilinogen
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Animalia
spellingShingle liver enzyme
porphobilinogen synthase
animal cell
article
breast cancer
enzyme kinetics
mouse
nonhuman
priority journal
Animal
Enzyme Stability
Heat
Hydrogen-Ion Concentration
Kinetics
Liver
Male
Mammary Neoplasms, Experimental
Mice
Mice, Inbred BALB C
Porphobilinogen
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Animalia
Navone, N.M.
Polo, C.F.
Frisardi, A.L.
Batlle, A.M.D.C.
Mouse mammary carcinoma δ-aminolevulinate dehydratase
topic_facet liver enzyme
porphobilinogen synthase
animal cell
article
breast cancer
enzyme kinetics
mouse
nonhuman
priority journal
Animal
Enzyme Stability
Heat
Hydrogen-Ion Concentration
Kinetics
Liver
Male
Mammary Neoplasms, Experimental
Mice
Mice, Inbred BALB C
Porphobilinogen
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Animalia
description 1. 1. Aminolevulinate dehydratase (ALA-D) was studied in crude extract from mouse mammary carcinoma, normal mouse liver and tumour bearing mouse liver. 2. 2. A Michaelis-Menten behaviour and Km values between 0.24 and 0.31 mM were obtained for the enzyme in either source. 3. 3. In all three tissues there was a linear relationship between porphobilinogen formation and incubation time, up to 120 min, ALA-D was thermostable and optimum pH was at 6.8. 4. 4. There seems to be no structural alterations in tumoural ALA-D as compared with the enzyme from liver of both normal and tumour bearing mice. © 1990.
format JOUR
author Navone, N.M.
Polo, C.F.
Frisardi, A.L.
Batlle, A.M.D.C.
author_facet Navone, N.M.
Polo, C.F.
Frisardi, A.L.
Batlle, A.M.D.C.
author_sort Navone, N.M.
title Mouse mammary carcinoma δ-aminolevulinate dehydratase
title_short Mouse mammary carcinoma δ-aminolevulinate dehydratase
title_full Mouse mammary carcinoma δ-aminolevulinate dehydratase
title_fullStr Mouse mammary carcinoma δ-aminolevulinate dehydratase
title_full_unstemmed Mouse mammary carcinoma δ-aminolevulinate dehydratase
title_sort mouse mammary carcinoma δ-aminolevulinate dehydratase
url http://hdl.handle.net/20.500.12110/paper_03050491_v96_n4_p729_Navone
work_keys_str_mv AT navonenm mousemammarycarcinomadaminolevulinatedehydratase
AT polocf mousemammarycarcinomadaminolevulinatedehydratase
AT frisardial mousemammarycarcinomadaminolevulinatedehydratase
AT batlleamdc mousemammarycarcinomadaminolevulinatedehydratase
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