Seasonal change and prolonged anoxia affect the kinetic properties of phosphofructokinase and pyruvate kinase in oysters

2000 ◽  
Vol 170 (4) ◽  
pp. 285-293 ◽  
Author(s):  
S. C. Greenway ◽  
K. B. Storey
Keyword(s):  
Pyruvate Kinase ◽  
Seasonal Change ◽  
Kinetic Properties

Effects of seasonal change and prolonged anoxia on metabolic enzymes of Littorina littorea

2001 ◽  
Vol 79 (5) ◽  
pp. 907-915 ◽  
Author(s):  
Steven C Greenway ◽  
Kenneth B Storey
Keyword(s):  
Pyruvate Kinase ◽  
Digestive Gland ◽  
Seasonal Change ◽  
Littorina Littorea ◽  
Kinetic Properties ◽  
Enzyme Kinetic ◽  
Seasonal Differences ◽  
Exposure In Vivo ◽  
Induced Changes

The effects of seasonal change (July versus November) and prolonged anoxia (N2 atmosphere at 5 or 10°C for 6 days) exposure in vivo on the activities of 18 enzymes, as well as the kinetic properties of phosphofructokinase (PFK) and pyruvate kinase (PK), were investigated in foot muscle and digestive gland of the marine periwinkle Littorina littorea L. Seasonal differences in enzyme maximal activities were tissue-specific, with generally increased activities during the summer and changes in a greater number of enzymes in digestive gland than in foot muscle. Seasonal differences in the kinetic properties of PFK and PK were observed in both tissues. PK from digestive gland of winter animals showed a much higher S0.5 for phosphoenolpyruvate and stronger changes in enzyme kinetic properties in response to anoxia than did the enzyme in summer animals; this may suggest the presence of seasonal isozymes. The effects of anoxia were tissue- and season-specific. Anoxia exposure during the winter induced a greater number of changes in enzyme maximal activities in foot muscle than in digestive gland. Anoxia-induced changes in the kinetic properties of both PFK and PK were also seen in both organs. For PK, these changes were consistent with less active enzyme forms in the anoxic state. Hence, both seasonal and environmental (anoxia) factors influence enzyme maximal activities and kinetic properties in L. littorea.

Kinetic properties of the muscular pyruvate kinase from the giant marine barnacle, Austromegabalanus psittacus (Molina, 1782) (Cirripedia, Balanomorpha)

Crustaceana ◽  
2005 ◽  
Vol 78 (10) ◽  
pp. 1203-1218
Author(s):  
Daniel López ◽  
Robert Simpfendörfer ◽  
Karin Oelckers ◽  
David Nash
Keyword(s):  
Pyruvate Kinase ◽  
Kinetic Properties

Effects of anoxia on the extra- and intracellular acid-base status in the land snail helix lucorum (L.): lack of evidence for a relationship between pyruvate kinase down-regulation and acid-base status

1999 ◽  
Vol 202 (12) ◽  
pp. 1667-1675
Author(s):  
B. Michaelidis ◽  
A. Pallidou ◽  
P. Vakouftsi
Keyword(s):  
Pyruvate Kinase ◽  
Active Form ◽  
Land Snail ◽  
Land Snails ◽  
Kinetic Properties ◽  
Acid Base ◽  
Down Regulation ◽  
Helix Lucorum ◽  
End Products ◽  
Acid Base Status

The aims of the present study were to describe a possible correlation between the regulation of the key glycolytic enzyme pyruvate kinase and the acid-base status in the haemolymph and in several other tissues of land snails during anoxia. To illustrate whether such a relationship exists, we determined (i) the acid-base variables in the haemolymph and tissues of the land snail Helix lucorum, (ii) the kinetic properties of pyruvate kinase from several tissues and (iii) the levels of the anaerobic end-products d-lactate and succinate in the haemolymph and tissues of aerobic and anoxic Helix lucorum. The results showed that the pH of haemolymph (pHe) decreased significantly over the first 20 h of anoxia and then recovered slowly towards control values. A similar pattern was observed for intracellular pH (pHi), which decreased significantly over the first 16 h of anoxia and slowly returned towards control levels. The reduction and recovery of pHi and pHe seem to reflect the rate of anaerobic metabolism. The main anaerobic end-products, d-lactate and succinate, accumulated rapidly during the initial stages of anoxia and more slowly as anoxia progressed. The decrease in the rate of accumulation of anaerobic end-products during prolonged anoxia was due to the conversion of tissue pyruvate kinase to a less active form. The results demonstrate a correlation between pyruvate kinase down-regulation and the recovery of acid-base status in the haemolymph and the tissues of land snails during anoxia.

Postnatal regulation of canine oxygen delivery: control of erythrocyte 2,3-DPG levels

1982 ◽  
Vol 242 (4) ◽  
pp. H500-H506
Author(s):  
P. A. Mueggler ◽  
J. A. Black
Keyword(s):  
Pyruvate Kinase ◽  
Oxygen Affinity ◽  
Kinetic Properties ◽  
Intracellular Activity ◽  
Slow Decline ◽  
Blood Oxygen Affinity ◽  
Intracellular Concentrations ◽  
Glycolytic Rate ◽  
2,3 Dpg

The oxygen affinity of canine blood changes markedly following birth. These changes are correlated with alterations in the intracellular concentration of 2,3-diphosphoglycerate (2,3-DPG). We have examined the control of erythrocyte glycolysis by measurements of intracellular enzymes and intermediates, and we have identified the component responsible for regulation of 2,3-DPG concentration and hence blood oxygen affinity during canine postnatal development. The concentration of 2,3-DPG could be regulated entirely by the enzymes of the Rapoport-Luebering shunt. We have not detected any alterations in the levels or intracellular activity of 2,3-DPG mutase or 2,3-DPG phosphatase during development; therefore postnatal changes of 2,3-DPG must be a result of changes in the intracellular concentrations of 1,3-diphosphoglycerate (1,3-DPG) that are controlled by other reactions in the glycolytic pathway. Neither low intracellular concentrations of glucose, the glycolytic substrate, nor an inherently low glycolytic rate can account for the low 2,3-DPG levels at birth. 1,3-DPG concentrations and hence 2,3-DPG concentrations are controlled by the activity of pyruvate kinase, which acts as a glycolytic sink reaction. The intracellular activity of pyruvate kinase decreases during the first 50-60 days of age and causes the accumulation of 2,3-DPG. There is a subsequent change in the in vivo kinetic properties of the enzyme, giving increased intracellular activity and resulting in the slow decline of 2,3-DPG concentrations toward normal adult values.

Some kinetic properties of skeletal muscle pyruvate kinase from air-breathing and water-breathing fish of the Amazon

1978 ◽  
Vol 56 (4) ◽  
pp. 751-758 ◽  
Author(s):  
J. H. A. Fields ◽  
W. R. Driedzic ◽  
C. J. French ◽  
P. W. Hochachka
Keyword(s):  
Skeletal Muscle ◽  
Pyruvate Kinase ◽  
Adenosine Diphosphate ◽  
Kinetic Properties ◽  
Air Breathing ◽  
Hoplias Malabaricus ◽  
Arapaima Gigas ◽  
Saturation Kinetics ◽  
Muscle Pyruvate Kinase ◽  
Hoplerythrinus Unitaeniatus

The kinetic properties of pyruvate kinase from skeletal muscle were studied in two species of air-breathing fish, Hoplerythrinus unitaeniatus and Arapaima gigas, and two species of water-breathing fish, Hoplias malabaricus and Osteoglossum bicirrhosum. It was found that the enzymes from Hoplias and Hoplerythrinus showed hyperbolic saturation kinetics for all substrates, were activated slightly by fructose 1,6-diphosphate, and were inhibited by phosphocreatine and citrate. The enzyme from Hoplias was inhibited by alanine, whereas the enzyme from Hoplerythrinus was not. The enzymes from Arapaima and Osteoglossum showed hyperbolic saturation kinetics for adenosine diphosphate, but the saturation kinetics for phusphoenol-pyruvate were sigmoidal. These enzymes were strongly activated by fructose 1,6-diphosphate and strongly inhibited by alanine, the former completely reversing the inhibition by the latter. Phosphocreatine and citrate were also found to be inhibitors of these enzymes, but the inhibition by phosphocreatine was not reversed by additions of fructose 1,6-diphosphate. The enzymes from the water-breathing fish were more sensitive to inhibition by alanine than were those from the air-breathing fish, but in other respects the enzymes were very similar.

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