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Temperature-dependence of fish muscle AMP-aminohydrolase

Published online by Cambridge University Press:  11 May 2009

W. Makarewicz
Affiliation:
Department of Biochemistry, Medical School, Gdańsk-6, Poland

Extract

The effect of temperature on the rate of reaction catalysed by crude muscle AMP-aminohydrolase from two species of elasmobranch and two species of teleost fish has been investigated at low substrate concentration in the range of temperature 5–50 °C.

The enzyme from teleost fish shows a very broad temperature optimum around 30 °C. The reaction rate of the enzyme from elasmobranch fish is strongly dependent on temperature. The optimum temperature for the enzyme from thornback ray lies around 40 °C. Both crude and 500-fold purified AMP-aminohydrolase from thornback ray show the same temperature-dependence.

Type
Research Article
Copyright
Copyright © Marine Biological Association of the United Kingdom 1968

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References

REFERENCES

Davison, J. A. & Richards, A. G., 1954. Muscle apyrase activity as a function of temperature in the cockroach, crayfish and minnow. Archs Biochem. Biophys., Vol. 48, pp. 484–6.Google Scholar
Gornall, A. G., Bardawill, C. J., & David, M. M., 1949. Determination of serum proteins by means of the biuret reaction. J. biol. Chem., Vol. 177, pp. 751–66.CrossRefGoogle ScholarPubMed
Hancock, R. L., 1965. Earthworm adenosine triphosphatase—a temperature study of poikilotherm enzyme. Aust. J. biol. Sci. Vol. 18, pp. 707–10.CrossRefGoogle ScholarPubMed
Kalckar, H. M., 1947. Differential spectrophotometry of purine compounds by means of specific enzymes. J. biol. Chem., Vol. 167, pp. 429–43, 445–59, 461–75.CrossRefGoogle ScholarPubMed
Lee, Y. P., 1957. 5-Adenylic acid deaminase. I. Isolation of the crystalline enzyme from rabbit skeletal muscle. J. biol. Chem., Vol. 227, pp. 987–92.Google Scholar
Levy, H. M., Sharon, N., Ryan, E. M. & Koshland, D. E. Jr., 1962. Effect of temperature on the rate of hydrolysis of adenosine triphosphate and inosine triphosphate by myosin with and without modifiers. Evidence for a change in protein conformation. Biochim. biophys. Acta, Vol. 56, pp. 118–26.CrossRefGoogle ScholarPubMed
Partmann, W., 1955. Zur Frage der Temperaturabhängigkeit der ATP-Spaltung in der Kalt und Warmblütermuskulatur. Biochem. Z., Bd. 326, pp. 260–9.Google Scholar
Steinbach, H. B., 1949. Temperature coefficients of muscle apyrase system. J. cell, comp. Physiol., Vol. 33, pp. 123–31.CrossRefGoogle Scholar
Zydowo, M., Makarewicz, W., Umiastowski, J. & Purzycka, J., 1965. Temperature dependence of AMP deamination catalysed by muscle extracts from homeothermic and poikilothermic animals. Ada biochim. polon., Vol. 12, pp. 319–25.Google Scholar