Environmentally low-temperature kinetic and thermodynamic study of lactate dehydrogenase from Atlantic cod (G. morhua) using a 96-well microplate technique
| العنوان: | Environmentally low-temperature kinetic and thermodynamic study of lactate dehydrogenase from Atlantic cod (G. morhua) using a 96-well microplate technique |
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| المؤلفون: | Maxim Zakhartsev, Hans O. Pörtner, Ronny Blust |
| المصدر: | Analytical biochemistry EPIC3Analytical Biochemistry, 330, pp. 10-20 |
| بيانات النشر: | Elsevier BV, 2004. |
| سنة النشر: | 2004 |
| مصطلحات موضوعية: | 030310 physiology, Biophysics, Analytical chemistry, Activation energy, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, symbols.namesake, Lactate dehydrogenase, Spectrophotometry, medicine, Animals, Gadus, Muscle, Skeletal, Molecular Biology, 030304 developmental biology, Arrhenius equation, 0303 health sciences, Temperature control, L-Lactate Dehydrogenase, biology, medicine.diagnostic_test, Cell Biology, biology.organism_classification, Microplate Reader, Freezing point, Cold Temperature, Kinetics, Gadus morhua, chemistry, symbols, Thermodynamics |
| الوصف: | Analyses of temperature-dependent kinetic parameters in enzymes extracted from tissues of ectothermic animals are usually carried out within the range of physiological temperatures (0-40 degrees C). However, multisample spectrophotometers (so-called microplate readers) with efficient wide-range temperature control (including cooling) have previously been unavailable. This limits the statistical quality of the measurements. A temperature-controlled microplate was designed for a 96-well microplate reader to overcome this limitation. This so-called T-microplate is able to control assay temperature between the freezing point of a liquid sample and 60 degrees C with high stability and accuracy in any data acquisition mode. At 4 degrees C the accuracy of the temperature control was +/-0.1 degrees C and temperature homogeneity across the microplate was +/-0.3 degrees C. As examples, analyses of the temperature dependence of Michaelis-Menten (K'(PYR)(m) and substrate inhibition (K'(PYR)(si) constants for pyruvate, of the maximal rate of reaction (V'(max), of the apparent Arrhenius activation energy (E(A), and of the Gibbs free-energy change (deltaG) of lactate dehydrogenases from muscle of Atlantic cod Gadus morhua acclimated to 4 degrees C are described. The large dataset obtained allowed evaluation of a new mechanism of metabolic compensation in response to seasonal temperature change. |
| وصف الملف: | application/pdf |
| تدمد: | 0003-2697 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f879837c6a1e331b058984fed0e3818aTest https://doi.org/10.1016/j.ab.2004.03.070Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....f879837c6a1e331b058984fed0e3818a |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00032697 |
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