Modification of pyruvate kinase and lactate dehydrogenase in foot muscle of the sea mussel Mytilus galloprovincialis under anaerobiosis and recovery
| العنوان: | Modification of pyruvate kinase and lactate dehydrogenase in foot muscle of the sea mussel Mytilus galloprovincialis under anaerobiosis and recovery |
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| المؤلفون: | A.V. Spichenkov, Volodymyr I. Lushchak, T.V. Bahnjukova |
| المصدر: | Brazilian Journal of Medical and Biological Research, Vol 30, Iss 3, p 381 (1997) Brazilian Journal of Medical and Biological Research, Vol 30, Iss 3, Pp 381-385 (1997) |
| بيانات النشر: | Associação Brasileira de Divulgação Científica, 1997. |
| سنة النشر: | 1997 |
| مصطلحات موضوعية: | Pyruvate dehydrogenase kinase, Physiology, muscle, Immunology, Biophysics, Biochemistry, Cofactor, pyruvate kinase, chemistry.chemical_compound, Lactate dehydrogenase, Animals, Seawater, General Pharmacology, Toxicology and Pharmaceutics, lcsh:QH301-705.5, chemistry.chemical_classification, lcsh:R5-920, L-Lactate Dehydrogenase, biology, Muscles, General Neuroscience, anaerobiosis, lactate dehydrogenase, Cell Biology, General Medicine, Mussel, biology.organism_classification, Enzyme assay, Mytilus, Bivalvia, Enzyme, chemistry, Mytilus galloprovincialis, lcsh:Biology (General), biology.protein, property modification, lcsh:Medicine (General), Pyruvate kinase |
| الوصف: | The modification of pyruvate kinase (PK) and lactate dehydrogenase (LDH) activity in foot muscle of the mussel Mytilus galloprovincialis during exposure to air and recovery in water was investigated. In the course of exposure to air, the activity of these enzymes measured at high and low substrate concentrations showed successive increases and decreases. Returning the mussels to water after exposure to air affected enzyme activity in a manner similar to anaerobiosis. When measuring at saturated concentrations of substrates and substrate and coenzyme for PK and LDH, respectively, the maximum activation of PK (37%) was observed at 4 h of animal exposure to air, and for LDH (67%) at 6 h exposure to air. During 24 h of exposure of animals to air, PK activity practically reached the stock level, while LDH was still activated (148%). The change in lactate dehydrogenase activity in mussel muscle during anoxia and recovery is described here for the first time. Variation in pyruvate kinase activity during exposure to air and recovery is linked to the alteration of half-maximal saturation constants and maximal velocity for both substrates. The possible role of reversible phosphorylation in the regulation of pyruvate kinase and lactate dehydrogenase properties is discussed. |
| اللغة: | English |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3424be7bf4b13f0b8728041fe9a691e0Test http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000300012Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....3424be7bf4b13f0b8728041fe9a691e0 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |