Studies on avian heart pyruvate kinase during development

Harris, Winfred; Days, Richard; Johnson, Clifton; Finkelstein, I.; Stallworth, Jerry; Hubert, Charles

doi:10.1016/0006-291x(77)91498-x

Cited by 10 publications

(1 citation statement)

References 8 publications

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“…Recently, it has been shown that, whereas pyruvate kinases from skeletal muscle of the adult rat and chicken exhibit no response to fructose bisphosphate, the enzymes from the foetal rat and chicken muscle are stimulated by this compound (Guguen-Guillouzo et al, 1977;Harris et al, 1977). A marked activation by fructose bisphosphate was observed on the 15th day of gestation in the rat, but this was almost nonexistent by the 21st day.…”

Section: Animalmentioning

confidence: 99%

Maximum activities and effects of fructose bisphosphate on pyruvate kinase from muscles of vertebrates and invertebrates in relation to the control of glycolysis

Zammit

Beis

Newsholme

1978

Biochemical Journal

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1. Comparison of the maximum activities of pyruvate kinase with those of phosphofructokinase in a large number of muscles from invertebrates and vertebrates indicates that, in general, in any individual muscle, the activity of pyruvate kinase is only severalfold higher than that of phosphofructokinase. This is consistent with the suggestion, based on massaction ratio data, that the pyruvate kinase reaction is non-equilibrium in muscle. However, the range of activities of pyruvate kinase in these muscles is considerably larger than that of phosphofructokinase.' This difference almost disappears if the enzyme activities from muscles that are known to possess an.anaerobic 'succinate pathway' are excluded. It is suggested that, in these muscles, phosphofructokinase provides glycolytic residues for both pyruvate kinase (i.e. -glycolysis) and phosphoenolpyruvate carboxykinase (i.e. the succinate pathway). This is. supported by a negative correlation between the activity ratio, pyruvate kinase/phosphofructokinase, and the activities of nucleoside diphosphokinase in these muscles, since high.activities of nucleoside diphosphokinase are considered to indicate the presence of the succinate pathway. 2. The effect of fructose bisphosphate on the activities of pyruvate kinase from many different muscles was studied. The stimulatory effect of fructose bisphosphate appears to be lost whenever an efficient system for supply of oxygen to the muscles is developed (e.g. insects, squids, birds and mammals). This suggests that activation of pyruvate kinase is important in the co-ordinated regulation of glycolysis in anaerobic or hypoxic conditions, when the change in glycolytic flux during the transition from rest to activity needs to be large in order to provide sufficient energy for the contractile activity. However, lack of this effect in the anaerobic muscles of the birds and mammals suggests that another metabolic control may exist for avian and mammalian pyruvate kinase in these muscles.

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Section: Animalmentioning

confidence: 99%

Maximum activities and effects of fructose bisphosphate on pyruvate kinase from muscles of vertebrates and invertebrates in relation to the control of glycolysis

Zammit

Beis

Newsholme

1978

Biochemical Journal

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Developmental changes in the pyruvate kinase isozymes of coho salmon

Guderley¹,

Cardenas²

1979

J. Exp. Zool.

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Pyruvate kinase exists as two major isozymes in coho salmon. As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearence of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distincy. Both forms are dubject to fructose 1,6-bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. While the immunological data indicates considerable divergence in structure, the kinetic parameters of the two forms have remained relatively similar.

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Developmental Changes in Membrane Electrical Properties of the Heart

Sperelakis¹

1989

Physiology and Pathophysiology of the Heart

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Studies on avian heart pyruvate kinase during development

Cited by 10 publications

References 8 publications

Maximum activities and effects of fructose bisphosphate on pyruvate kinase from muscles of vertebrates and invertebrates in relation to the control of glycolysis

Maximum activities and effects of fructose bisphosphate on pyruvate kinase from muscles of vertebrates and invertebrates in relation to the control of glycolysis

Developmental changes in the pyruvate kinase isozymes of coho salmon

Developmental Changes in Membrane Electrical Properties of the Heart

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