Abstract
The myosin ATPase activity of the flexor muscle of an estuarine crab, Scylla serrata, was studied in relation to salinity adaptation. The enzyme is activated more by calcium than by magnesium; it exhibits maximum activity at pH 9.0, and substrate inhibition above 0.5 mM ATP. The enzyme activity increases in crabs adapted to higher salinities. The enzyme from normal (70% sea water) crabs shows two pH optima; one at pH 7.0, the other at pH 9.0. The neutral optimum shifts to pH 6.0 upon adaptation to full strength sea water, but disappears upon adaptation to 25% sea water. The enzyme from normal crabs shows an optimum at 30 °C; adaptation to full strength sea water raises this optimum to 38 °C, whereas adaptation to 25% sea water decreases it to 24 °C. These changes are discussed in relation to estuarine conditions.
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Colowick, S. P. and N. O. Kaplan: Methods in enzymology, Vol. 3, 1154 pp. New York: Academic Press 1957.
Ebashi, S. and M. Endo: Calcium and muscle contraction. In: Progress in biophysics and molecular biology, Vol. 18, pp 123–186. Ed. by J. A. V. Butlee and D. Noble. Oxford: Pergamon Press 1969.
Fiske, C. H. and Y. Subbarow: The colorimetric determination of phosphorus. J. biol. Chem. 66, 375–400 (1925).
Florkin, M.: Ecology and metabolism. In: Physiology of Crustacea, pp 395. Ed. by T. H. Waterman. New York: Academic Press 1960.
Hasselbach, W. and G. Schneider: Der L-Myosin- und Aktingehalt des Kaninchenmuskels. Biochem. Z. 321, 462–475 (1951).
Kinne, O.: Non-genetic adaptation to temperature and salinity. Helgoländer wiss. Meeresunters. 9, 433–458 (1964a).
—: The effects of temperature and salinity on marine and brackish-water animals. II. Salinity and temperaturesalinity combinations. Oceanogr. mar. Biol. A. Rev. 2, 281–339 (1964b).
—: Physiological aspects of animal life in estuaries with special reference to salinity. Neth J. Sea Res. 3, 222–244 (1966).
Kinne, O.: Non-genetic adaptation in Crustacea. In: Proceedings of Symposium on Crustacea. Pt 3. Symp. Ser. mar. biol. Ass. India 2, 999–1007 (1967).
Krishnamurthi, B.: Gross morphology and histology of nephridia in four species of polychaetes. Proc. Indian Acad. Sci B 57, 195–209 (1963).
—: Physiological studies on Marphysa gravelyi. 8. Tissue respiration. Helgoländer wiss. Meeresunters. 16, 179–187 (1967).
— and S. Krishnaswamy: Physiological studies on Marphysa gravelyi: regulation of chlorides, sodium, potassium and total free amino acids. Helgoländer wiss. Meeresunters. 12, 315–328 (1965).
—: Physiological studies on Marphysa gravelyi: regulation of chlorides body fluid concentration. Zool. Jb. (allg. Zool. Physiol.) 72, 316–326 (1966).
Mahler, H. R. and E. H. Cordes: Biological chemistry, 872 pp. New York: Harper & Row 1966.
Maruyama, K.: Contractile protein from crayfish tail muscle. Biol. Bull. mar. biol. Lab., Woods Hole 114, 95–105 (1958).
McShan, W. H., S. Kramer and N. N. Olson: Adenosine triphosphatase activity of American cockroach and wood-roach thoracic muscle. Biol. Bull. mar. biol. Lab., Woods Hole 108, 45–53 (1955).
Mommaerts, W. F. H. M. and K. Seraidarian: A study of the adenosine triphosphatase activity of myosin and actomyosin. J. gen. Physiol. 30, 401–409 (1947).
Panikkar, N. K.: Physiological aspects of adaptation to estuarine conditions. Proc. Indo-Pacif. Fish. Coun. 2, 168–175 (1950).
Perry, S. V.: Myosin adenosine triphosphatase. In: Methods in enzymology, Vol. 2, pp 582–583. Ed. by S. P. Colowick and N. O. Kaplan. New York: Academic Press 1955.
Poglazov, B. F.: The structure and functions of contractile proteins, 321 pp. Transl. Ed. J. A. Stekol. New York: Academic Press 1966.
Precht, H.: Über die Resistenzadaptation wechselwarmer Tiere an extreme Temperaturen und ihre Ursachen. Helgoländer wiss. Meeresunters. 9, 329–411 (1964).
Prosser, C. L.: Comparative physiology in relation to evolutionary theory. In: Evolution after Darwin, Vol. 1, pp. 569–594. Ed. by Sol Tax and C. Callender. Chicago: University Press 1960.
—: Temperature. In: Comparative animal physiology, pp 238–284. Ed. by C. L. Prosser and F. A. Brown Jr. Philadelphia: W. B. Saunders Co. 1961.
Ramamurthi, R.: Succinic dehydrogenase activity in a fresh water crab in relation to salinity stress. Comp. Biochem. Physiol. 19, 645–648 (1966).
Rao, K. P.: Oxygen consumption as a function of size and salinity in Metapenaeus monoceros (Fab) from marine and brackish water environments. J. exp. Biol. 35, 307–313 (1958).
Shaw, J.: Ionic regulation in the muscle fibres of Carcinus maenas. 1. The electrolyte composition of single fibres. J. exp. Biol. 32, 383–396 (1955).
Ushakov, B. P.: Thermostability of cells and proteins of poikilotherms and its significance in speciation. Physiol. Rev. 44, 518–560 (1964).
Venkatramiah, A.: Studies on the hydrobiology of the Krishna estuary: salinity, adaptive physiology of selected estuarine species. Doct. diss. Sri Venkateswara Univ., Tirupati A.P., India 1966.
De Villafranca, G. W.: Adenosine triphosphatase activity of squid mantle muscle (Loligo pealii). Biol. Bull. mar. biol. Lab., Woods Hole 108, 113–119 (1955).
Wells, G. P. and I. C. Ledingham: Physiological effects of hypotonic environment. 1. The action of hypotonic saline on isolated rhythmic preparations from polychaete worms (Arenicola marina, Nereis diversicolor and Perinereis cultrifeur). J. exp. Biol. 17, 337–352 (1940).
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Communicated by N. K. Panikkar, Panji
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Krishnamoorthy, R.V., Venkatramiah, A. Myosin ATPase activity in an estuarine decapod crustacean, Scylla serrata, as a function of salinity adaptation. Marine Biology 4, 345–348 (1969). https://doi.org/10.1007/BF00350364
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DOI: https://doi.org/10.1007/BF00350364