Abstract
Activity of NADP+-dependent isocitrate dehydrogenase (ICDH) of the white dorsal muscle of Idus idus L. was determined by special analysis, under optimum homogenisation, centrifugation and cuvette conditions. The experimental conditions differed considerably from those used for the investigation of NADP+-ICDH activity in mammals by Bücher et al. (1964). Daily measurements of activity over a period of 10 days revealed variations in enzyme activity which are difficult to explain. However, the variations are smaller than those established in earlier tests. In order to obtain statistically valid results, the highest possible number of test fishes (at least 10 individuals for each measurement) must be investigated over a period of 5 to 10 days. NADP+-ICDH of individuals acclimated to 10°C showed 28% higher specific and non-specific activity than that of fish maintained at 20°C (experimental temperature 25°C). At 5 different adaptation temperatures, increasing activities were observed with decreasing adaptation temperature (compensation). These measurements were made over a period of 5 successive days.
Similar content being viewed by others
Zitierte literatur
Bass, A., D. Bridiczka, P. Eyer, S. Hofer and D. Pette: Metabolic differentiation of distinct muscle types at the level of enzymatic organisation. Eur. J. Biochem. 10, 198–206 (1969).
Beisenherz, G., H. J. Boltze, Th. Bücher, R. Czok, K. K. Garbade, E. Meyer-Arendt und G. Pfleiderer: Diphosphofructose-Aldolase, Phosphoglyceraldehyd-Dehydrogenase, Milchsäure-Dehydrogenase, Glycerophosphat-Dehydrogenase und Pyruvat-Kinase aus Kaninchenmuskulatur in einem Arbeitsgang. Z. Naturf. (Sect. B) 8, 555–577 (1953).
Bergmeyer, H. U. (Ed.): Methoden der enzymatischen Analyse. Bd. I, 1085 pp. Weinheim/Bergstraße: Verlag Chemie 1970.
Braun, K., H. Künnemann und H. Laudien: Der Einfluß von Temperaturänderungen auf Enzyme der Fischmuskulatur. Versuche mit Rhodeus amarus. Mar. Biol. 7, 59–70 (1970).
Bücher, Th., W. Luh und D. Pette: Einfache und zusammengesetzte optische Tests mit Pyridinnucleotiden. In: Handbuch der physiologisch- und pathologisch-chemischen Analyse. Vol. 6 A. pp 292–339 und 387–414. Hrsgb. von E. F. Hoppe-Seyler und H. Thierfelder. Berlin: Springer-Verlag 1964.
Colmann, R. F.: Distinct SH-groups responsible for catalytic and conformational changes in isocitrate dehydrogenase. Fedn Proc. Fedn Am. Socs exp. Biol. 29, p. 665 (1970).
Cooper, I., P. A. Srere, M. Tabachnick und E. Racker: The oxidative pentose phosphate cycle. II. Quantitative determination of intermediates and enzymes. Archs Biochem. Biophys. 74, 306–314 (1958).
Keller, R.: Über eine portionskonstante Enzymgruppe beim Flußkrebs (Cambarus affinis Say). Naturwissenschaften 8, p. 192 (1965).
Künnemann, H., H. Laudien und H. Precht: Der Einfluß von Temperaturänderungen auf Enzyme der Fischmuskulatur. Versuche mit Goldorfen Idus idus. Mar. Biol. 7, 71–81 (1970).
Lehmann, J.: Über die Abhängigkeit der Enzymaktivitäten im Rumpfmuskel der Goldorfen (Idus idus L.) von der Vorbehandlungstemperatur. Int. Revue ges. Hydrobiol. 55, 413–429 (1970a).
— Veränderungen der Enzymaktivitäten nach einem Wechsel der Adaptationstemperatur, untersucht am Seitenrumpfmuskel des Goldfisches (Carassius auratus L.). Int. Revue ges. Hydrobiol. 55, 763–781 (1970b).
Love, R. M.: The chemical biology of fishes. 547 pp. London and New York: Academic Press 1970.
Lowry, O. H., N. J. Rosebrough, A. L. Farr and R. I. Randall: Protein measurement with the folin phenol reagent. J. biol. Chem. 193, 265–275 (1951).
Malessa, P.: Beiträge zur Temperaturadaptation des Aales (Anguilla vulgaris). III. Höhe und Verteilung der Aktivität von Succinodehydrogenase und Cytochromoxydase im Seitenmuskel juveniler und adulter Tiere. Mar. Biol. 3, 143–158 (1969).
Northrop, D. B. and W. W. Cleland: The kinetics of metal ion activators for TPN-isocitrate dehydrogenase. Fedn Proc. Fedn Am. Socs exp. Biol. 29, p. 408 (1970).
Ochoa, S.: Isocitric dehydrogenase system (TPN) from pig heart. In: Methods in enzymology, Vol. 1. pp 699–704. Ed. by S. Colowick and N. O. Kaplan. New York: Academic Press 1955.
Pette, D., M. Klingenberg and Th. Bücher: Comparable and specific proportions in the mitochondrial enzyme activity pattern. Biochem. biophys. Res. Commun. 7, 425–432 (1962).
—, W. Luh and Th. Bücher: A constant-protein group in the enzyme activity pattern of the Embden-Meyerhof-chain. Biochem. biophys. Res. Commun. 7, 419–424 (1962).
Precht, H.: Der Einfluß, normaler “Temperaturen auf Lebensprozesse bei wechselwarmen Tieren unter Ausschluß der Wachstums- und Entwicklungsprozesse. Helgoländer wiss. Meeresunters. 18, 487–548 (1968).
Prosser, C. L.: Acclimation of poikilothermic vertebrates to low temperatures. In: Comparative physiology of temperature regulation, Part I. pp 1–44. Ed. by I. P. Hannon and E. Viereck. Proc. Symp. Arctic Biol. Med., Arctic Aeromedical Laboratory, Fort Wainwright, Alaska 1962.
—: Metabolic and central nervous acclimation of fish to cold. In: The cell and environmental temperature, pp 375–383. Ed. by A. S. Troshin. Oxford: Pergamon Press 1967.
Rose, Z. B.: Studies on the mechanism of action of isocitric dehydrogenase. J. biol. Chem. 235, 928–933 (1960).
Author information
Authors and Affiliations
Additional information
Communicated by O. Kinne, Hamburg
Rights and permissions
About this article
Cite this article
Passia, D. NADP+-isocitrat-dehydrogenase aus Idus idus (Pisces: Cyprinidae). I. Aktivität als funktion der adaptationstemperatur. Mar. Biol. 23, 197–204 (1973). https://doi.org/10.1007/BF00389485
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00389485