Artículo
Abstract:
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.
Registro:
| Documento: | Artículo |
| Título: | Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
| Autor: | Sancovich, H.A.; Batlle, A.M.C.; Grinstein, M. |
| Filiación: | Cátedra de Química Biológica 1, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Perú, 272 Buenos Aires, Argentina |
| Palabras clave: | 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 |
| Año: | 1969 |
| Volumen: | 191 |
| Número: | 1 |
| Página de inicio: | 130 |
| Página de fin: | 143 |
| DOI: | http://dx.doi.org/10.1016/0005-2744(69)90322-2 |
| Título revista: | BBA - Enzymology |
| ISSN: | 00052744 |
| CAS: | isomerase, 9013-19-8; lyase, 9055-04-3; porphyrin, 24869-67-8; Ammonium Compounds; Isomerases, EC 5.; Lyases, EC 4.; Porphyrins; Pyrroles |
| PDF: | https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00052744_v191_n1_p130_Sancovich.pdf |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v191_n1_p130_Sancovich |
Citas:
---------- APA ----------
Sancovich, H.A., Batlle, A.M.C. & Grinstein, M. (1969) . Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme. BBA - Enzymology, 191(1), 130-143.http://dx.doi.org/10.1016/0005-2744(69)90322-2
---------- CHICAGO ----------
Sancovich, H.A., Batlle, A.M.C., Grinstein, M. "Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme" . BBA - Enzymology 191, no. 1 (1969) : 130-143.http://dx.doi.org/10.1016/0005-2744(69)90322-2
---------- MLA ----------
Sancovich, H.A., Batlle, A.M.C., Grinstein, M. "Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme" . BBA - Enzymology, vol. 191, no. 1, 1969, pp. 130-143.http://dx.doi.org/10.1016/0005-2744(69)90322-2
---------- VANCOUVER ----------
Sancovich, H.A., Batlle, A.M.C., Grinstein, M. Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme. 1969;191(1):130-143.http://dx.doi.org/10.1016/0005-2744(69)90322-2
