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O-pyrocatechuic acid carboxy-lyase from Aspergillus niger
Archives of Biochemistry and Biophysics, 1967Abstract O -Pyrocatechuic acid (2,3-dihydroxybenzoic acid) carboxylyase (E.C. 4.1.1.), enzyme involved in the biosynthesis of catechol by Aspergillus niger , has been extracted from the acetone powders of mycelial mats grown in the presence of l -tryptophan and purified 815-fold by precipitation of nucleic acids, fractionation with ammonium ...
P V, Rao, K, Moore, G H, Towers
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Studies on Porphyrinogen Carboxy-Lyase from Chick Embryo Liver
Enzyme, 1984The purpose of the present work was to find the optimal conditions for the assay of chick embryo liver porphyrinogen carboxy-lyase. The enzyme activity was studied as a function of protein and substrate concentrations, time, pH value and incubation temperature.
M C, Taira, L C, San Martín de Viale
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Stereochemistry of porphyrinogen carboxy-lyase reaction in haem biosynthesis
Journal of the Chemical Society, Chemical Communications, 1975Stereospecifically deuteriated and tritiated succinate was incorporated into the acetate residues of uroporphyrinogen III which on decarboxylation generated asymmetric methyl groups in coproporphyrinogen III and then in haem; degradation of the latter yielded chiral acetate deriving from the C and D rings of haem and configurational analysis of this ...
Graham F. Barnard, Muhammad Akhtar
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Glyoxylate carboxy-lyase activity in the unicellular green alga gloemonas SP.
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract Glyoxylate carboxy-lyase (also known as glyoxylate carboligase, systematic name: glyoxylate carboxy-lase (dimerizing and reducing)) activity has been demonstrated in cell-free extracts prepared from the photoautotrophically grown unicellular green alga Gloeomonas.
S S, Badour, E R, Waygood
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Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract Several properties of porphyrinogen carboxy-lyase from normal chicken erythrocytes were studied. 1. 1. The utilization of the substrate uroporphyrinogen (8-COOH), and the formation of intermediate products (porphyrinogens of 7-, 6- and 5-COOH) and the final product coproporphyrinogen (4-COOH) were investigated as function of time and ...
R C, Garcia +3 more
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Clinica Chimica Acta, 1980
Red cell porphyrinogen carboxy-lyase activity was measured using uroporphyrinogen III as substrate in 18 normal persons, 7 male patients with porphyria cutanea tarda, 3 female patients with erythropoietic protoporphyria and 2 female patients with variegate porphyria.
M C, Ríos de Molina +3 more
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Red cell porphyrinogen carboxy-lyase activity was measured using uroporphyrinogen III as substrate in 18 normal persons, 7 male patients with porphyria cutanea tarda, 3 female patients with erythropoietic protoporphyria and 2 female patients with variegate porphyria.
M C, Ríos de Molina +3 more
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Archives of Biochemistry and Biophysics, 1975
Abstract Uridine 5′-(α- d -glucopyranosyluronic acid pyrophosphate) (UDPGluUA) cyclase [UDP GluUA → uridine 5′-(α- d -apio- d -furanosyl pyrophosphate) + CO 2 ] was purified 71-fold from Lemna minor by a four-step procedure. When this purification procedure was used some, but not all, of the UDPGluUA carboxy-lyase [UDPGluUA → uridine 5′-(α- d ...
D L, Gustine, D H, Yuan, P K, Kindel
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Abstract Uridine 5′-(α- d -glucopyranosyluronic acid pyrophosphate) (UDPGluUA) cyclase [UDP GluUA → uridine 5′-(α- d -apio- d -furanosyl pyrophosphate) + CO 2 ] was purified 71-fold from Lemna minor by a four-step procedure. When this purification procedure was used some, but not all, of the UDPGluUA carboxy-lyase [UDPGluUA → uridine 5′-(α- d ...
D L, Gustine, D H, Yuan, P K, Kindel
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Biochimica et Biophysica Acta (BBA) - Biomembranes, 1976
A sensitive and quantitative assay for 3-octaprenyl-4-hydroxybenzoate carboxy-lyase has been developed. This enzyme, which catalyses the third reaction in ubiquinone biosynthesis in Escherichia coli, was partially purified and some of its properties determined.
R A, Leppik, I G, Young, F, Gibson
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A sensitive and quantitative assay for 3-octaprenyl-4-hydroxybenzoate carboxy-lyase has been developed. This enzyme, which catalyses the third reaction in ubiquinone biosynthesis in Escherichia coli, was partially purified and some of its properties determined.
R A, Leppik, I G, Young, F, Gibson
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Biochemie und Physiologie der Pflanzen, 1977
Summary Orotidine-5′-phosphate: pyrophosphate-phosphoribosyltransferase and orotidine-5′-phosphate: carboxy-lyase were characterized in a crude extract from Euglena gracilis. Z The coupled enzyme reaction was measured by 14 CO 2 release from [7- 14 C]-orotic acid. Characteristics of the enzyme system are an apparent K m value for orotate of 17 μ
W. Rattke, G.-J. Krauss
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Summary Orotidine-5′-phosphate: pyrophosphate-phosphoribosyltransferase and orotidine-5′-phosphate: carboxy-lyase were characterized in a crude extract from Euglena gracilis. Z The coupled enzyme reaction was measured by 14 CO 2 release from [7- 14 C]-orotic acid. Characteristics of the enzyme system are an apparent K m value for orotate of 17 μ
W. Rattke, G.-J. Krauss
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