Summary
Concentrations of glycolytic intermediates, lactate, adenine nucleotides, inorganic phosphate, phosphoarginine and citrate have been estimated after various periods of valve closure (Table 1 and Fig. 1). Mass action ratios of enzyme steps involved in the metabolism of these components are compared with their equilibrium constants. This reveals glycogen phosphorylase, phosphofructokinase, hexosediphosphatase and pyruvate kinase catalyze non-equilibrium reactions. The first three enzymes possess relatively low activities (Table 2).
From the changes in concentrations of the glycolytic intermediates it is concluded that phosphofructokinase controls the carbon flow during the first hours after valve closure, whereas later on the rate of conversion of phosphoenolpyruvate is determining this flow. In skeletal muscle phosphofructokinase controls the carbon flow during the whole period of exercise.
The concentrations of ADP, AMP and inorganic phosphate increase, whereas the concentrations of ATP, phosphoarginine and citrate decrease during valve closure (Table 1 and Fig. 2). In contrast to skeletal muscle, these changes do not result in a strong increase in the glycolytic flux.
There is a much greater potential for ATP hydrolysis by the myofibrillar ATPase system than is actually realized by the adductor muscle during valve closure.
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References
Beis, I., Newsholme, E.A.: The contents of adenosine nucleotides, phosphagens and some glycolytic intermediates in resting muscles from vertebrates and invertebrates. Biochem. J.152, 23–32 (1975)
Bernt, E., Bergmeyer, H.U., Möllering, H.: Creatine. In: Methods of enzymatic analysis. Bergmeyer, H.U. (ed.), pp. 1772–1776. New York, London: Academic Press 1974
Coleman, N.: The heart rate and activity of bivalve molluses in their natural habitats. Oceanogr. Mar. Biol. Ann. Rev.12, 301–313 (1974)
Cornell, N.W., Leadbetter, M.G., Veech, R.L.: Modification in the enzymatic assay for inorganic phosphate. Anal. Biochem.95, 524–526 (1979)
Ebberink, R.H.M., Zurburg, W., Zandee, D.I.: The energy demand of the posterior adductor muscle ofMytilus edulis in catch during exposure to air. Mar. Biol. Lett.1, 23–31 (1979)
Gutman, I., Wahlefeld, A.W.: L-(+)-Lactate. In: Methods of enzymatic analysis. Bergmeyer, H.U. (ed.), pp. 1464–1468. New York, London: Academic Press 1974
Jaworek, D., Gruber, W., Bergmeyer, H.U.: Adenosine-5′-triphosphate. In: Methods of enzymatic analysis. Bergmeyer, H.U. (ed.), pp. 2097–2101. New York, London: Academic Press 1974a
Jaworek, D., Gruber, W., Bergmeyer, H.U.: Adenosine-5′-triphosphate and adenosine-5′-monophosphate. In: Methods of enzymatic analysis. Bergmeyer, H.U. (ed.), pp. 2127–2131. New York, London: Academic Press 1974b
Lamprecht, W., Stein, P., Heinz, F., Weisser, H.: Creatine phosphate. In: Methods of enzymatic analysis. Bergmeyer, H.U. (ed.), pp. 1777–1781. New York, London: Academic Press 1974
Lehninger, A.L.: Biochemistry. New York: Worth Publishers 1975
Mangum, C., Winkle, W. van: Responses of aquatic invertebrates to declining oxygen conditions. Am. Zool.13, 529–541 (1973)
Newsholme, E.A., Beis, I., Leech, A.R., Zammit, V.A.: The role of creatine kinase and arginine kinase in muscle. Biochem. J.172, 533–537 (1978)
Ramaiah, A.: Pasteur effect and phosphofructokinase. Curr. Top. Cell. Regul.8, 297–345 (1974)
Rolleston, F.S.: A theoretical background to the use of measured concentrations of intermediates in study of the control of intermediary metabolism. Curr. Top. Cell. Regul.5, 47–75 (1972)
Sacktor, B., Hurlbut, E.C.: Regulation of metabolism in working musclein vivo II. J. Biol. Chem.241, 632–634 (1966)
Sacktor, B., Wormser-Shavit, E.: Regulation of metabolism in working musclein vivo I. J. Biol. Chem.241, 624–631 (1966)
Szent-Györgyi, A.C., Cohen, C., Kendrick-Jones, J.: Paramyosin and the filaments of molluscan ‘catch’ muscles. J. Mol. Biol.56, 239–258 (1971)
Wilson, J.E., Sacktor, B., Tiekert, C.G.:In situ regulation of glycolysis in tetanized cat skeletal muscle. Arch. Biochem. Biophys.120, 542–546 (1967)
Wijsman, T.C.M.: pH fluctuations inMytilus edulis L. in relation to shell movements under aerobic and anaerobic conditions. In: Proc. 9th Europ. Mar. Biol. Symp. Barnes, H. (ed.), pp. 139–149. Aberdeen: Aberdeen University Press 1975
Wijsman, T.C.M.: Adenosine phosphate and energy charge in different tissues ofMytilus edulis L. under aerobic and anaerobic conditions. J. Comp. Physiol.107, 129–140 (1976)
Zammit, V.A., Newsholme, E.A.: The maximum activities of hexokinase, phosphorylase, phosphofructokinase, glycerol phosphate dehydrogenase, lactate dehydrogenase, octopine dehydrogenase, phosphoenolpyruvate carboxykinase, nucleoside diphosphatekinase, glutamate-oxaloacetate transaminase and argininekinase in relation to carbohydrate utilization in muscles from marine invertebrates. Biochem. J.160, 447–462 (1976)
Zwaan, A. de, Wijsman, T.C.M.: Anaerobic metabolism in Bivalvia (Mollusca). Characteristics of anaerobic metabolism. Comp. Biochem. Physiol.54B, 313–324 (1976)
Zwaan, A. de, Zandee, D.I.: Body distribution and seasonal changes in the glycogen content of the sea musselMytilus edulis L. Comp. Biochem. Physiol.43A, 53–58 (1971)
Zurburg, W., Kluytmans, J.H., Pieters, P., Zandee, D.I.: The influence of seasonal changes on energy metabolism inMytilus edulis (L.). — II. Organ specificity. In: Cyclic phenomena in marine plants and animals. Naylor, E., Hartnoll, R.G. (eds.), pp. 293–300. Oxford: Pergamon Press 1979
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Ebberink, R.H.M., de Zwaan, A. Control of glycolysis in the posterior adductor muscle of the sea musselMytilus edulis . J Comp Physiol B 137, 165–171 (1980). https://doi.org/10.1007/BF00689216
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DOI: https://doi.org/10.1007/BF00689216