Biochemical and physiological properties of the lactate dehydrogenase allozymes of the Brazilian teleost, Leporinus friderici, Anostomidae, Cypriniformes

Panepucci, L.; Schwantes, Maria Luiza B.; Schwantes, Arno Rudi

doi:10.1016/0305-0491(87)90490-1

Cited by 4 publications

(4 citation statements)

References 22 publications

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“…Some components present in the fertilizer industrial effluent interact together and produce toxicity to aquatic organisms for example the interaction between dissolve oxygen and elevated ammonia has been shown to alter the respiratory physiology of fresh water fish (Pickering and Pottinger 1987). These findings indicated that the inhibitory effect of industrial effluent on the activity of LDH may be mediated via formation of enzyme-inhibitor complex leading to impairment of carbohydrate metabolism (Panepucci et al 1984(Panepucci et al , 1987Copper and Somero 1990;Sharma and Gopal 1995).…”

Section: Resultsmentioning

confidence: 96%

Fertilizer Industry Effluent Induced Biochemical Changes in Fresh water Teleost, Channa striatus (Bloch)

Yadav

Gopesh

Pandey

et al. 2007

Bull Environ Contam Toxicol

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The industrial activities pose threat to the life of aquatic organisms in many ways. This research communication presents an account of the impact of fertilizer industry effluent upon the levels of protein and the activity of lactate dehydrogenase (EC 1.1.1.28, LDH), a terminal key enzyme in glycolytic pathway, in different organs of a fresh water teleost fish, Channa striatus (Bloch). The fish exposed to different sublethal concentrations of fertilizer industry effluent (3.5, 4.7 and 7.0% v/v) equivalent to 1/20th, 1/15th and 1/10th of LC(50) value (70% v/v) for varying treatment periods (96 h and 15 days) exhibited decrease in the level of protein (8-76%) in different organs of the effluent treated fish. At highest effluent concentration (7% v/v) treatment for short (96 h) or long (15 days) duration, the liver of the fish registered significant (p < 0.001) decrease (62-76%) in protein content as compared to control, whereas other organs of the fish showed only 38-52% decrease in the level of protein. The industrial effluent also caused marked reduction in the activity of LDH in different fish tissues when compared to the control. The treatment of fish with 7% effluent concentration for 96 h caused 78% decrease (p < 0.001) in the LDH activity in fish muscle whereas after 15 days the effect was maximum in fish brain as it exhibited 86% decrease (p < 0.001) in LDH activity as compared to control. The effect of effluent on the activity of LDH and protein content in different body tissues of the fish was dependent on concentration and duration of exposure. The significant reductions in the activity of LDH and level of protein in fish tissues due to treatment with the fertilizer industry effluent indicated the possibility of impairments in energy metabolism and protein turnover, respectively, in C. striatus.

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Section: Resultsmentioning

confidence: 96%

Fertilizer Industry Effluent Induced Biochemical Changes in Fresh water Teleost, Channa striatus (Bloch)

Yadav

Gopesh

Pandey

et al. 2007

Bull Environ Contam Toxicol

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“…Studies on exposure of fishes acclimated to different dissolved oxygen concentrations did not give a single answer for enzyme responses (Shaklee et al, 1977;Almeida-Val & Hochachka, 1993;. There is an extensive background of work in general and specific properties of lactate dehydrogenases (LDH) (Wilson 1977;Graves & Somero, 1982;Panepucci et al, 1984Panepucci et al, , 1987Coppes & Somero, 1990) and in the soluble form of malate dehydrogenases (cMDH) (Shaklee et al, 1977;Schwantes & Schwantes, 1982a, b;Farias & Almeida-Val, 1992;Lin & Somero, 1995a, b). Lactate dehydrogenase (LDH, lactate; NAD-oxidoredutase, EC 1.1.1.27) is among the most extensively studied glycolitic enzyme.…”

Section: Introductionmentioning

confidence: 99%

Changes in lactate dehydrogenase and malate dehydrogenase activities during hypoxia and after temperature acclimation in the armored fish, Rhinelepis strigosa (Siluriformes, Loricariidae)

et al. 2000

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Lactate (LDH) and malate dehydrogenase (MDH) of white skeletal muscle of fishes acclimated to 20, 25 and 30 degrees C and thereafter submitted to hypoxia were studied in different substrate concentrations. Significant differences for LDH and MDH of white muscle enzyme activities are described here for the first time in Rhinelepis strigosa of fishes acclimated to 20 degrees C and submitted to hypoxia for six hours. LDH presented a significant decrease in enzyme affinity for pyruvate in acute hypoxia, for fishes acclimated to 20 degrees C and an increase for fishes acclimated to 30 degrees C.

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“…On the other hand, B-isoforms are characteristically more susceptible to substrate inhibition, channeling more pyruvate into the Kreb's cycle and functioning mainly as lactate oxidases. The apparent K m (pyr) values obtained here have been compared with other fish LDH K m values (Wuntch and Goldberg, 1970;Panepucci et al, 1987;Coppes and Somero, 1990;Almeida-Val et al, 1991). All were found to be similar to K m values obtained for muscle and heart LDH or their purified isoforms.…”

Section: Discussionmentioning

confidence: 70%

“…Lactate dehydrogenase (LDH; EC 1.1.1.27) isoforms in fish, coded at two or three loci, LDH-A*, LDH-B* and LDH-C*, have been the subject of many studies (Markert and Faulhaber, 1965;Panepucci et al, 1984Panepucci et al, , 1987Coppes et al, 1987;Almeida-Val et al, 1990Fenerich-Verani et al, 1990;Ferreira et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Lactate dehydrogenase of Mugil sp. (Mugilidae, Perciformes). Lack of electrokinetic, thermostability and kinetic differences among individuals with different number of scales

Santos

Schwantes

2000

Genet. Mol. Biol.

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The scale number in lateral sets (SNS) of Mugil sp. (Mugilidae, Perciformes) collected in the lagoon-estuarine region of Cananéia, State of São Paulo ranges from 33 to 39. Electrokinetic, kinetic and thermostability properties of lactate dehydrogenase (LDH) were tested to determine if individuals with different SNS correspond to different species or populations of mullet. As in many other teleosts, LDH-A*, LDH-B*, and LDH-C* loci were detected. Through a two-fold serial dilution method applied to 10 different tissues of Mugil sp., a bidirectionally divergent expression of these loci was suggested. No association among LDH electrophoretic pattern, thermal inactivation, kinetic responses and different SNS was observed. The apparent K m (pyr) values obtained here were similar to K m values obtained by other authors for muscle and heart LDH or their purified isoforms. The effect of NaCl on K m and V max values of Mugil sp. (35 and 39 SNS individuals) indicates that this salt behaves as a competitive inhibitor, since it decreases enzyme-substrate affinity. Thus, electrokinetic and thermostability behavior, K m and V max values and the effect of NaCl do not permit us to consider these mullets, with SNS ranging from 33 to 39, as belonging to different populations or species.

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Biochemical and physiological properties of the lactate dehydrogenase allozymes of the Brazilian teleost, Leporinus friderici, Anostomidae, Cypriniformes

Cited by 4 publications

References 22 publications

Fertilizer Industry Effluent Induced Biochemical Changes in Fresh water Teleost, Channa striatus (Bloch)

Fertilizer Industry Effluent Induced Biochemical Changes in Fresh water Teleost, Channa striatus (Bloch)

Changes in lactate dehydrogenase and malate dehydrogenase activities during hypoxia and after temperature acclimation in the armored fish, Rhinelepis strigosa (Siluriformes, Loricariidae)

Lactate dehydrogenase of Mugil sp. (Mugilidae, Perciformes). Lack of electrokinetic, thermostability and kinetic differences among individuals with different number of scales

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