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Lactate and malate dehydrogenase in the fan-shell associated shrimp, Pontonia pinnophylax (Otto): Effects of temperature and urea |
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| Authors: | G Laganà S Giacobbe C Mannucci S Ficarra U Leuzzi |
| Institution: | a Department of Organic and Biological Chemistry, University of Messina Salita Sperone, Messina, Italy b Department of Animal Biology and Marine Ecology, University of Messina Salita Sperone, Messina, Italy c Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic |
| Abstract: | In Pontonia pinnophylax (Otto), a crustacean decapod inhabiting the mantle cavity of Pinna nobilis L. (Bivalvia: Pteriomorpha), the lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) activity, and their electrophoretic patterns, were compared in relation to heat and urea inactivation. Activity was higher in LDH than in MDH, and the electrophoretic patterns showed a predominance of LDH-A4 and the presence of both mitochondrial and cytosolic MDH. Heat incubation reduced both enzymatic activities, but more MDH. Also all isozymes showed different heat sensitivity, with anodic forms more heat-resistant than cathodic ones, either in LDH as in MDH. Urea treatment caused also a higher inactivation of the most cathodic isozymes, but MDH appeared more resistant than LDH at 2 M urea. The high polymorphism of these enzymes suggests an adaptation of Pontonia metabolism to hypoxic conditions; moreover, the different isozyme stability grade should be functional to contrast environmental variability. |
| Keywords: | Crustacean decapods Environmental adaptation Enzyme thermostability Isozymes Urea denaturation |
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