Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Muscle biopsy samples were collected from the middle gluteal muscle of seven horses undergoing a nine-month endurance training programme. Samples were collected before the programme began and again after three, six and nine months of training. A fifth sample was collected three months after training ceased. Serial muscle sections were reacted histochemically for myosin adenosine triphosphatase after either acid (pH 4.3 and 4.6) or alkaline (pH 10.3) pre-incubation, and muscle fibres identified as type I, IIA, IIB or IIC. The oxidative capacity of individual fibres was assessed, using the reduced nicotinamide dinucleotide tetrazolium reductase stain, and the number of intermyofibrillar capillaries adjacent to each fibre was counted after staining, using the alpha-amylase periodic acid Schiff technique. Biochemical analyses involved the fluorometric measurement of the enzymes citrate synthase, 3-hydroxy acyl CoA dehydrogenase and lactate dehydrogenase as markers of end terminal oxidative, beta oxidative and glycolytic potential, respectively. There was an increase in the percentage of type IIB fibres having high nicotinamide dinucleotide tetrazolium reductase staining after three months training. This increase persisted throughout the period of training and during the period without training. There was an increase in the number of capillaries adjacent to type IIB fibres after six and nine months training. These had returned to near pre-training numbers after three months without training. There were increases in the activities of citrate synthase and 3-hydroxy acyl CoA dehydrogenase after three months training. The activities of both enzymes continued to rise throughout training and the highest activities were attained after nine months.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of a nine-month endurance training programme on muscle composition in the horse. 367 37

Biopsy samples were obtained from the middle gluteal muscle of 10 Thoroughbred horses undergoing a commercial race-training program. Samples were obtained before the program began and again after 6 and 12 weeks of training. All horses had raced at least once by the 12th week of training. Serial sections of muscle were examined histochemically for myosin adenosinetriphosphatase after either acid (pH 4.3 and 4.6) or alkaline (pH 10.3) preincubation, and then muscle fibers were identified as types I, IIA, IIB, or IIC. The oxidative capacity of individual fibers was assessed, using the reduced nicotinamide dinucleotide tetrazolium-reductase stain, and the number of intermyofibrillar capillaries adjacent to each fiber were counted after staining, using the alpha-amylase-periodic acid-Schiff technique. Biochemical analyses involved the fluorometric measurement of 3 enzymes--citrate synthase, 3-hydroxy-acyl coenzyme A dehydrogenase, and lactate dehydrogenase--as markers of end terminal oxidative, beta-oxidative, and glycolytic potentials, respectively. Changes in fiber-type percentages did not occur in response to training. There was a significant (P less than 0.01) increase in the percentage of type IIB fibers, having high nicotinamide dinucleotide-tetrazolium reductase staining after 12 weeks of training. Alterations in the number of capillaries adjacent to each fiber type did not occur during the training period. There were increases in the activities of both citrate synthase and 3-hydroxy-acyl coenzyme A dehydrogenase after 6 weeks (P less than 0.05) and 12 weeks (P less than 0.001) of training. Alterations in the activity of lactate dehydrogenase did not occur in response to training.
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PMID:Effects of training on muscle composition in horses. 394 89

A new, weakly hydrophobic, high-performance liquid chromatography column has been developed for the separation of native proteins based on their relative hydrophobicities. Starting with a covalently bound, hydrophilic polyamine matrix, packing materials were synthesized through acylation with anhydrides and acid chlorides of increasing chain length to obtain increasingly hydrophobic surfaces. Proteins in aqueous buffers were induced to bind hydrophobically to the columns by the use of high salt concentrations in the mobile phase. Elution was achieved by decreasing the ionic strength of the solvent in a linear gradient. A mixture of cytochrome c, conalbumin, and beta-glucosidase was used as a standard to test the resolving power of newly synthesized columns. On a 4-cm butyrate column, baseline resolution was achieved in 20 min with a gradient of 3.0 mu sodium sulfate in 0.1 M potassium phosphate buffer, pH 7.0, to water. The static loading capacity for each column was determined using a hemoglobin binding assay. Capacities normally ranged between 150 and 180 mg of hemoglobin per gram of support. Since proteins are not denatured in hydrophobic interaction chromatography, enzymes eluted from the column retained enzymatic activity. Samples of alpha-amylase and beta-glucosidase ranging in size from 10 to 200 micrograms were recovered from the butyrate column with greater than 92% enzymatic activity in all cases. In a single trial, the enzyme citrate synthase was recovered from the benzoate column with 92% retention of enzymatic activity.
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PMID:High-performance hydrophobic interaction chromatography of proteins. 642 67

Enzymes from cold-adapted species are significantly more active at low temperatures, even those close to zero Celsius, but the rationale of this adaptation is complex and relatively poorly understood. It is commonly stated that there is a relationship between the flexibility of an enzyme and its catalytic activity at low temperature. This paper gives the results of a study using molecular dynamics simulations performed for five pairs of enzymes, each pair comprising a cold-active enzyme plus its mesophilic or thermophilic counterpart. The enzyme pairs included alpha-amylase, citrate synthase, malate dehydrogenase, alkaline protease and xylanase. Numerous sites with elevated flexibility were observed in all enzymes; however, differences in flexibilities were not striking. Nevertheless, amino acid residues common in both enzymes of a pair (not present in insertions of a structure alignment) are generally more flexible in the cold-active enzymes. The further application of principle component analysis to the protein dynamics revealed that there are differences in the rate and/or extent of opening and closing of the active sites. The results indicate that protein dynamics play an important role in catalytic processes where structural rearrangements, such as those required for active site access by substrate, are involved. They also support the notion that cold adaptation may have evolved by selective changes in regions of enzyme structure rather than in global change to the whole protein.
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PMID:Cold-active enzymes studied by comparative molecular dynamics simulation. 1723 16

Response of two wheat cultivars (Triticum aestivum cv. YM 158 and NM 9) to the herbicide chlorotoluron and the effect of two forms of dissolved organic matter on the chlorotoluron toxicity to the plants were characterized. Treatment with chlorotoluron at 10-50 microg/ml inhibited the seed germination and a dose-response was observed. The inhibition of seed germination was correlated to the depression of alpha-amylase activities. To identify whether chlorotoluron induced oxidative damage to wheat plants, the malondlaldehyde (MDA) content and electrolyte leakage were measured. Results showed that both MDA content and electrolyte leakage in the chlorotoluron-treated roots significantly increased. Activities of several key enzymes were measured that operate in citric acid cycle and carbohydrate metabolic pathway. Inhibited activities of citrate synthase and NADP-isocitrate dehydrogenase were observed in the chlorotoluron-treated roots as compared to control plants. We also examined malate dehydrogenase and phosphoenolpyruvate carboxylase in wheat roots exposed to 30 gg/ml chlorotoluron. However, none of the enzymes showed significant changes in activities. Application of 160 microg/ml dissolved organic matter (DOM) extracted from non-treated sludge (NTS) and heat-expanded sludge (HES) in the medium with 30 microg/ml chlorotoluron induced an additive inhibition of seed germination and plant growth. The inhibition of growth due to the DOM treatment was associated with the depression of activities of alpha-amylase, citrate synthase and NADP-isocitrate dehydrogenase, as well as the increase in malondlaldehyde content and electrolyte leakage. These results suggested that the presence of DOM might enhance the uptake and accumulation of chlorotoluron, and thus resulted in greater toxicity in wheat plants. The two forms of DOM exhibited differences in regulation of chlorotoluron toxicity to the wheat plants. Treatments with DOM-NTS induced greater toxicity to plants as compared to those with DOM-HES. In addition to DOM affecting chlorotoluron-induced toxicity to wheat plants, the cultivars could have also contributed to differences. Generally, NM-9 showed a higher sensitivity to chlorotoluron than YM 158 either in the absence or in the presence of DOM.
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PMID:Effect of dissolved organic matter on the toxicity of chlorotoluron to Triticum aestivum. 2005 May 56