Controlling the highest lactate dehydrogenase activity known in nature

In the shipjack, Euthynnus pelamis, white muscle appears to possess a powerful anaerobic capacity as well as a significant carbohydrate based aerobic potential. Lactate dehydrogenase occurs at higher activities than found thus far anywhere else in nature and clearly functions in anaerobic glycolysis. Alpha-glycerophosphate dehydrogenase also occurs in unusually high activities and appears to play a role in aerobic glycolysis. Regulation of these two reactions is accomplished by temperature, pH, and creatine phosphate levels. High temperature, low pH, and low creatine phosphate levels all appear to favor lactate dehydrogenase over alpha-glycerophosphate dehydrogenase; low temperature, high pH, and high creatine-phosphate levels, all expected during the quiescent state in this species, and when metabolism in aerobic, all favor alpha-glycerophosphate dehydrogenase activity.

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Lactate Metabolism in Fish

Journal of the Marine Biological Association of the United Kingdom ◽

10.1017/s002531540004652x ◽

1969 ◽

Vol 49 (1) ◽

pp. 209-223 ◽

Cited By ~ 44

Author(s):

P. R. Dando

Keyword(s):

Lactate Dehydrogenase ◽

Dehydrogenase Activity ◽

Blood Lactate ◽

White Muscle ◽

Glycolytic Enzymes ◽

Lactate Metabolism ◽

Lactate Dehydrogenase Activity ◽

Lactate And Pyruvate

The activity of lactate dehydrogenase was measured in the livers of 36 species of fish. These species could be divided into two groups, those with liver activities of more than 1000 mU/mg protein and those with activities of less than 100 mU/ mg protein. The lactate and pyruvate of samples of blood, muscle and liver from cod, plaice, bass and mackerel were determined. Samples were taken from ‘rested’ and trawled fish and from fish allowed to recover for 3 h after trawling. The rate of removal of lactate from the white muscle after capture in the trawl was not related to high blood and liver activities of lactate dehydrogenase. There was no relationship between the activities of nine of the glycolytic enzymes in the white muscle of cod and plaice and the liver lactate dehydrogenase activity. Little blood lactate appears to be taken up by the liver. It is concluded that the liver of cod, plaice and bass has a negligible role in metabolizing blood lactate.

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Adaptation to temporary muscle anoxia in Anurans: Activities of glycolytic enzymes in muscles from species differing in their ability to produce lactate during exercise

Australian Journal of Zoology ◽

10.1071/zo9770015 ◽

1977 ◽

Vol 25 (1) ◽

pp. 15 ◽

Cited By ~ 1

Author(s):

J Baldwin ◽

G Friedman ◽

H Lillywhite

Keyword(s):

Lactate Dehydrogenase ◽

Dehydrogenase Activity ◽

Energy Production ◽

Anaerobic Capacity ◽

Glycolytic Enzymes ◽

Lactate Dehydrogenase Activity ◽

Anaerobic Energy ◽

Specific Activities

Specific activities of the enzymes lactate dehydrogenase, phosphorylase, phosphofructokinase and hexokinase were determined in hind leg musculature taken from four species of anuran having different capacities for producing lactate during exercise. The specific activities of phosphorylase, phosphofructokinase, and the ratio phosphorylase: hexokinase were highest in animals having high increments of lactate following exercise, and lowest in those showing low increments. The specific activities of these glycolytic enzymes could possibly be used as an index of the reliance of different species on anaerobic energy production. Lactate dehydrogenase activity was not well correlated with anaerobic capacity.

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Transition from ectothermy to endothermy: the development of metabolic capacity in a bird ( Gallus gallus )

Proceedings of The Royal Society B Biological Sciences ◽

10.1098/rspb.2005.3333 ◽

2005 ◽

Vol 273 (1586) ◽

pp. 565-570 ◽

Cited By ~ 17

Author(s):

Frank Seebacher ◽

Tonia S Schwartz ◽

Michael B Thompson

Keyword(s):

Gene Expression ◽

Lactate Dehydrogenase ◽

Dehydrogenase Activity ◽

Aerobic Capacity ◽

Anaerobic Capacity ◽

Internal Heat ◽

Gallus Gallus ◽

Metabolic Capacity ◽

Lactate Dehydrogenase Activity ◽

Evolutionary Innovation

The evolution of endothermy is one of the most significant events in vertebrate evolution. Adult mammals and birds are delineated from their early ontogenetic stages, as well as from other vertebrates, by high resting metabolic rates and consequent internal heat production. We used the embryonic development of a bird ( Gallus gallus ) as a model to investigate the metabolic transition between ectothermy and endothermy. Increases in aerobic capacity occur at two functional levels that are regulated independently from each other: (i) upregulation of gene expression; and (ii) significant increases in the catalytic activity of the main oxidative control enzymes. Anaerobic capacity, measured as lactate dehydrogenase activity, is extremely high during early development, but diminishes at the same time as aerobic capacity increases. Changes in lactate dehydrogenase activity are independent from its gene expression. The regulatory mechanisms that lead to endothermic metabolic capacity are similar to those of ectotherms in their response to environmental change. We suggest that the phylogenetic occurrence of endothermy is restricted by its limited selective advantages rather than by evolutionary innovation.

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