Lactate Dehydrogenase Activity In Tissues Research Articles

Effects of Ancylostoma ceylanicum Infection on Lactate Dehydrogenase Activity in Tissues of Mesocricetus auratus

Aim: The present research aims to study the effects of Ancylostoma ceylanicum infection on lactate dehydrogenase activity in the tissues of Mesocricetus auratus. Methodology: In the current investigation, Ancylostoma ceylanicum, a hookworm was infected in the host, a hamster Mesocricetus auratus experimentally in laboratory conditions in Hyderabad from 1992 to 1996. The infected host was then studied using the parameters of Lactate dehydrogenase activity in various tissues. The Lactate Dehydrogenase content in M. auratus was investigated biochemically in both the infected and control samples. Results: The results revealed increased levels of Lactate dehydrogenase in the intestinal and muscle tissue of the infected host. Decreased LDH content in the liver, kidney, spleen, lungs, brain and serum was found in the infected host of Lactate Dehydrogenase as the anaerobic conditions prevail in the intestinal region of the host infected with hookworm infection. Conclusion: The present paper reveals the Lactate dehydrogenase content in Mesocricetus auratus infected with Ancylostoma ceylanicum as compared to control and its significance.

Effects of paraoxon on serum biochemical parameters and oxidative stress induction in various tissues of Wistar and Norway rats

This study investigates the effects of different doses of paroxon (POX), an active metabolite of the organophosphate pesticide parathion, on some serum biochemical parameters and induction of oxidative stress in various tissues of female Wistar and Norway rats. The rats were intraperitoneally treated with 0.3, 0.7, 1 and 1.5mg/kg of POX. The parameters were evaluated after 24h. The results showed that the decreased glutathione level and catalase, glutathione-S-transferase and lactate dehydrogenase activities in tissues of Wistar rat were higher than Norway rat at higher doses of POX. At these concentrations, POX increased superoxide dismutase activity, malondialdehyde level and some serum biochemical indices. In conclusion, POX induces the production of free radicals and oxidative stress in a dose-dependent manner. Induction of oxidative stress in POX-treated rats is in the order of brain>liver>heart> kidney>spleen. Wistar rat is found to be more sensitive to the toxicity of POX compared to Norway rat.

Temperature Dependence of the Lactate Dehydrogenase Activity in Tissues of the Black Sea Flatfishes

Temperature Dependence of the Lactate Dehydrogenase Activity in Tissues of the Black Sea Flatfishes

Individual Effects of Hydrostatic Pressure and Hypoxia on Lactate Dehydrogenase Activity in Tissues of Fishes with Different Parameters of Locomotor Function

Individual Effects of Hydrostatic Pressure and Hypoxia on Lactate Dehydrogenase Activity in Tissues of Fishes with Different Parameters of Locomotor Function

Characterization of two electrophoretic lactate dehydrogenase-A mutants in Mus musculus.

Two lactate dehydrogenase (LDH) mutations were recovered independently among offspring of ethylnitrosourea-treated male mice by screening for alterations of isoelectric focusing pattern in liver homogenates. Investigations of physicochemical and kinetic properties of the mutant enzymes indicated that the mutant traits resulted from point mutations at the Ldh-1 structural locus. Therefore, the new alleles were designated Ldh-1a-m5Neu and Ldh-1a-m6Neu, respectively. Both mutant alleles code for proteins which exhibit an altered stability to heat, in addition to changes in isoelectric focusing pattern and a reduction in anodal electrophoretic mobility. While LDH-Aa-m5Neu proteins are markedly less heat stable, LDH-Aa-m6Neu proteins are more heat stable than the wild-type enzyme. Furthermore, a small elevation of Km for pyruvate, a slightly reduced inhibition by high pyruvate concentrations, and a slight acidic shift of the pH activity profile distinguish LDH-Aa-m6Neu from both wild-type and LDH-Aa-m5Neu enzymes. Significant alterations of LDH activity were detected in some tissues from LDH-Aa-m5Neu individuals but not in those from LDH-Aa-m6Neu animals. Erythrocytes and blood of LDH-Aa-m5Neu mutants revealed activity levels which were reduced by approximately 6 and 13% compared with those of wild types in heterozygous and homozygous individuals, respectively. In addition, an elevation of approximately 6% in LDH activity was found in skeletal muscle in homozygous mutants. Consistent with the unaltered or only slightly altered LDH activity in tissues, the genetic as well as the physiological characterization yielded no easily detectable effects from either mutation on metabolism or fitness of the affected individuals.

The Effect of Seasonal Acclimatization on the Buffering Capacity and Lactate Dehydrogenase Activity in Tissues of the Freshwater Turtle Chrysemys Picta Marginata

ABSTRACT Freshwater turtles are remarkably tolerant of anoxic conditions, a tolerance essential for animals that spend much of their time submerged (Belkin, 1963). Many metabolic adaptations for efficient anaerobiosis have been elucidated in turtles, and are essential for allowing these animals not only to dive over a wide range of water temperatures (Gatten, 1981) but also to survive the long hibernation during winter in the higher latitudes (see Penney, 1987, for a review).

The effect of Ehrlich ascites tumour growth on lactate dehydrogenase activities in tissues and physiological fluids of tumour bearing mice

1. 1. Tumour growth kinetics and the activity of lactate dehydrogenase (LDH) in body fluids and host tissues were studied during the Ehrlich ascites tumour growth. The rate of tumour cell death was determined by measuring the loss of 125I from mice bearing [5- 125I]iodo-2′-deoxyuridine labelled tumour cells. 2. 2. The activity of LDH in serum increased progressively with increasing tumour mass during the first period of tumour growth, whereas that of cell free ascites fluid exhibited a peak level during early plateau phase growth. The analysis of LDH activity in cell free ascites fluid revealed that the increased LDH activity could only partly be attributed to a release from dead tumour cells. 3. 3. A marked increase in host liver LDH activity was observed. In addition, the growing tumour induced an increase in RNA synthesis activity and Kupffer cell proliferation in the liver. The LDH activity in skeletal muscle decreased significantly with increasing tumour mass. 4. 4. The observations show that the growing tumour exerts a marked effect on the metabolic activity of host tissues. It is suggested that an altered metabolism affects the cell membrane integrity of certain host tissues and causes a leakage of LDH molecules, which contributes to the increased extracellular LDH activity of tumour bearing animals.

CARDIAC METABOLISM.

CARDIAC METABOLISM.