Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
Kinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave d...
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todo:paper_00052744_v220_n3_p552_Llambias2023-10-03T14:03:25Z Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies Llambías, E.B.C. Del C. Batlle, A.M. ammonium derivative article binding site Ammonium Compounds Binding Sites Kinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave downward; Rs values were greater than 81; and in some cases the Hill coefficient was less than 1, indicating negative homotropic kinetics. Evidence also suggested that porphobilinogenase contains at least two substrate-binding sites per molecule of enzyme. It has also been found that ammonium ions act competitively on the first reaction of the porphobilinogenase. © 1970. Fil:Llambías, E.B.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. 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_00052744_v220_n3_p552_Llambias |
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 article binding site Ammonium Compounds Binding Sites |
spellingShingle |
ammonium derivative article binding site Ammonium Compounds Binding Sites Llambías, E.B.C. Del C. Batlle, A.M. Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies |
topic_facet |
ammonium derivative article binding site Ammonium Compounds Binding Sites |
description |
Kinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave downward; Rs values were greater than 81; and in some cases the Hill coefficient was less than 1, indicating negative homotropic kinetics. Evidence also suggested that porphobilinogenase contains at least two substrate-binding sites per molecule of enzyme. It has also been found that ammonium ions act competitively on the first reaction of the porphobilinogenase. © 1970. |
format |
JOUR |
author |
Llambías, E.B.C. Del C. Batlle, A.M. |
author_facet |
Llambías, E.B.C. Del C. Batlle, A.M. |
author_sort |
Llambías, E.B.C. |
title |
Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies |
title_short |
Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies |
title_full |
Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies |
title_fullStr |
Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies |
title_full_unstemmed |
Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies |
title_sort |
porphyrin biosynthesis in soybean callus. v. the porphobilinogen deaminase-uroporphyrinogen cosynthetase system. kinetic studies |
url |
http://hdl.handle.net/20.500.12110/paper_00052744_v220_n3_p552_Llambias |
work_keys_str_mv |
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1807322685164748800 |