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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Autor principal: Batlle, Alcira María del Carmen
Publicado: 1990
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v96_n4_p729_Navone
http://hdl.handle.net/20.500.12110/paper_03050491_v96_n4_p729_Navone
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spelling paper:paper_03050491_v96_n4_p729_Navone2023-06-08T15:30:25Z Mouse mammary carcinoma δ-aminolevulinate dehydratase Batlle, Alcira María del Carmen 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. 1990 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v96_n4_p729_Navone 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
Batlle, Alcira María del Carmen
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.
author Batlle, Alcira María del Carmen
author_facet Batlle, Alcira María del Carmen
author_sort Batlle, Alcira María del Carmen
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
publishDate 1990
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v96_n4_p729_Navone
http://hdl.handle.net/20.500.12110/paper_03050491_v96_n4_p729_Navone
work_keys_str_mv AT batllealciramariadelcarmen mousemammarycarcinomadaminolevulinatedehydratase
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