Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme
1. 1.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in...
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1969
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v191_n1_p130_Sancovich http://hdl.handle.net/20.500.12110/paper_00052744_v191_n1_p130_Sancovich |
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paper:paper_00052744_v191_n1_p130_Sancovich2023-06-08T14:29:53Z Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme Sancovich, Horacio Alberto Batlle, Alcira María del Carmen Grinstein, Moisés ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature 1. 1.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in the absence or presence of NH4+, which at high concentrations behaved as a noncompetitive inhibitor of the deaminase. As expected from Hill plots, n = 1 both in the absence or presence of NH4+. Instead, when activity of porpho bilinogenase is plotted versus porphobilinogen concentration, sigmoid curves are obtained; but the presence of NH4+ at different concentrations altered the kinetic parameters of this enzymic system, again showing normal kinetics. In addition, n values were found to be 2 for porphobilinogen per porphobilinogenase molecule and 1 in the presence of NH4+ which behaves as a competitive inhibitor of the isomerase. Results are discussed in relation to the allosteric theories of monod et al.1,2 and liver porphobilinogenase is proposed to be an allosteric protein. 3. 3.|The presence of an ultrafiltrable factor which stimulates uroporphyrinogen formation from porphobilinogen has been revealed. © 1969. Fil:Sancovich, H.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1969 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v191_n1_p130_Sancovich http://hdl.handle.net/20.500.12110/paper_00052744_v191_n1_p130_Sancovich |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature |
| spellingShingle |
ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature Sancovich, Horacio Alberto Batlle, Alcira María del Carmen Grinstein, Moisés Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| topic_facet |
ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature |
| description |
1. 1.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in the absence or presence of NH4+, which at high concentrations behaved as a noncompetitive inhibitor of the deaminase. As expected from Hill plots, n = 1 both in the absence or presence of NH4+. Instead, when activity of porpho bilinogenase is plotted versus porphobilinogen concentration, sigmoid curves are obtained; but the presence of NH4+ at different concentrations altered the kinetic parameters of this enzymic system, again showing normal kinetics. In addition, n values were found to be 2 for porphobilinogen per porphobilinogenase molecule and 1 in the presence of NH4+ which behaves as a competitive inhibitor of the isomerase. Results are discussed in relation to the allosteric theories of monod et al.1,2 and liver porphobilinogenase is proposed to be an allosteric protein. 3. 3.|The presence of an ultrafiltrable factor which stimulates uroporphyrinogen formation from porphobilinogen has been revealed. © 1969. |
| author |
Sancovich, Horacio Alberto Batlle, Alcira María del Carmen Grinstein, Moisés |
| author_facet |
Sancovich, Horacio Alberto Batlle, Alcira María del Carmen Grinstein, Moisés |
| author_sort |
Sancovich, Horacio Alberto |
| title |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| title_short |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| title_full |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| title_fullStr |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| title_full_unstemmed |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| title_sort |
porphyrin biosynthesis. vi. separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. porphobilinogenase an allosteric enzyme |
| publishDate |
1969 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v191_n1_p130_Sancovich http://hdl.handle.net/20.500.12110/paper_00052744_v191_n1_p130_Sancovich |
| work_keys_str_mv |
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| _version_ |
1768543973487411200 |