Results 121 to 130 of about 28,267 (166)
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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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International Journal of Biochemistry, 1980
Abstract 1. 1. It has been reported that hexachlorobenzene (HCB) in vivo produces hepatic porphyrinogen carboxy-lyase (PCL) decrease and pentachlorophenol (PCP) is one of its metabolites. In order to investigate if such decrease is due to an enzyme inhibitor present in the porphyric livers, the effects of the following additions on the normal rat
M C, Rios de Molina +2 more
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Abstract 1. 1. It has been reported that hexachlorobenzene (HCB) in vivo produces hepatic porphyrinogen carboxy-lyase (PCL) decrease and pentachlorophenol (PCP) is one of its metabolites. In order to investigate if such decrease is due to an enzyme inhibitor present in the porphyric livers, the effects of the following additions on the normal rat
M C, Rios de Molina +2 more
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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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The Journal of Nutrition, 1976
Activity of L-cysteinesulfinate carboxy-lyase (CSC) and persulfurase was measured in livers of rats fed 15% casein diets supplemented with (1) 0.53% cysteine, (2) 0.40% cysteine, (3) 0.40% cysteine + 0.10% sulfate, (4) 0.42% sulfate, or (5) 0.42% sulfate + 0.40% cysteine. The diets were fed to adult rats for 1 week and to weanling rats for periods of 1
B A, Whittle, C H, Lee
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Activity of L-cysteinesulfinate carboxy-lyase (CSC) and persulfurase was measured in livers of rats fed 15% casein diets supplemented with (1) 0.53% cysteine, (2) 0.40% cysteine, (3) 0.40% cysteine + 0.10% sulfate, (4) 0.42% sulfate, or (5) 0.42% sulfate + 0.40% cysteine. The diets were fed to adult rats for 1 week and to weanling rats for periods of 1
B A, Whittle, C H, Lee
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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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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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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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L-Arginine carboxy-lyase of higher plants and its relation to potassium nutrition
Phytochemistry, 1963Abstract On a fresh weight basis the mean agmatine content was found to be eight times as high, and the mean L -arginine carboxy-lyase (arginine decarboxylase) activity twice as high in leaves of potassium-deficient barley plants as in leaves of normal barley plants. A range of other plant species was also shown to accumulate agmatine and putrescine
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Plant and Cell Physiology, 2002
Uridine diphospho-D-glucuronate carboxy-lyase (UDP-D-xylose synthase; EC 4.1.1.35), which catalyzes the conversion of UDP-D-glucuronate to UDP-D-xylose, was purified to apparent homogenity from pea (Pisum sativum L.) seedlings. The pH optimum for enzyme activity was around 5-6, and the activity was not affected by exogeneously supplied NAD+ and NADH ...
Masaru, Kobayashi +4 more
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Uridine diphospho-D-glucuronate carboxy-lyase (UDP-D-xylose synthase; EC 4.1.1.35), which catalyzes the conversion of UDP-D-glucuronate to UDP-D-xylose, was purified to apparent homogenity from pea (Pisum sativum L.) seedlings. The pH optimum for enzyme activity was around 5-6, and the activity was not affected by exogeneously supplied NAD+ and NADH ...
Masaru, Kobayashi +4 more
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