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Chemical nature of monogenean sclerites. I. Stabilization of clamp-protein by formation of dityrosine

Published online by Cambridge University Press:  06 April 2009

K. Ramalingam
K. Ramalingam
Affiliation:
Department of Zoology, University of Madras, Chepauk, Madras-5, Tamil Nadu, India
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Extract

The clamp sclerites of Pricea multae and other higher monogeneans was fuchsin-positive in Mallory's and Masson's triple stain, and the staining was not affected by detanning agents, suggesting some form of stabilization in the protein. The sclerites were positive in Millon's, Morner's and Xanthoproteic tests for aromatic amino acids, but negative in tests for sulphydryl and disulphide groups. Quinone, phenol and phenol oxidase were absent. They stained with basic dyes such as toluidine blue and methylene blue in the pH range of 3·5–9·5, and also exhibited bluish fluorescence in u.v. light which was not affected by lipid solvents, indicating the presence of dityrosine and recalling the protein present in the ligament cuticle of insects. These features indicate that the clampprotein is stabilized by the formation of dityrosine. It is suggested that this protein may be responsible for the biological properties of the clamp sclerites. This mode of stabilization by tyrosyl residues of the protein, resulting in the formation of dityrosine, is the first record of its kind to be reported in platyhelminths.

Type
Research Article
Information
Parasitology , Volume 66 , Issue 1 , February 1973 , pp. 1 - 7
Copyright
Copyright © Cambridge University Press 1973

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References

Andersen, S. O., & Weis-Fogh, T., (1964). Resilin, a, rubber-like protein. Advances in Insect Physiology 2, 1–65.CrossRefGoogle Scholar
Blower, G., (1950). Aromatic tanning in the Myriapod cuticle. Nature 165, 569.CrossRefGoogle Scholar
Brown, C. H., (1950 a). Quinone tanning in the animal kingdom. Nature 165, 275.CrossRefGoogle ScholarPubMed
Brown, C. H., (1950 b). A review of the methods available for the determination of the types of forces stabilizing structural proteins in animals. Quarterly Journal of Microscopical Science 91, 331–9.Google ScholarPubMed
Bychowsky, B. E., (1957). Monogenetic Trematodes, Their Classification and Phytogeny, 509 pp. Moscow: Leningrad, Academy of Sciences, U.S.S.R.Google Scholar
Coles, G. C., (1966). Studies on resilin biosynthesis. Journal of Insect Physiology 12, 679–91.CrossRefGoogle ScholarPubMed
Declier, W., & Vercauteren, R., (1965). Activité phenoloxidasique dans les leucocytes de crabs au cours du cycle d'intermne. Cahiers de biologie marine 6, 163–72.Google Scholar
Dennell, R., & Malek, S. R. A., (1956). The cuticle of cockroach Periplaneta americana. IV. The hardening of the cuticle: Phenolic tanning. Proceedings of the Royal Society B 143, 427–34.Google Scholar
Feigl, F., (1960). Spot Tests in Organic Analysis. Amsterdam: Elsevier Publishing Company.Google Scholar
Guilbold, G. G., (1967). Kinetic methods of analysis. In Fluorescence: Theory, Instrumentation and Practice. New York: Mercer Dekker Inc.Google Scholar
Hackman, R. H., (1971). Distribution of cystine in a blow fly larval cuticle and stabilization of the cuticle by disulphide bonds. Journal of Insect Physiology 17, 1065–72.CrossRefGoogle Scholar
Hargis, W. J., & Oustinoff, P. C., (1961). Monogenetic Trematodes, Their Classification and Phytogeny. (English translation of B. E. Bychowsky, (1957).) Washington: American Institute of Biological Sciences.Google Scholar
Krishnan, G., (1953). On the cuticle of the scorpion Palamneus swammerdami. Quarterly Journal of Microscopical Science 94, 11–21.Google Scholar
Krishnan, G., (1969). Chemical components and mode of hardening of the cuticle of Collembola. Acta histochemica 34, 212–28.Google ScholarPubMed
Krishnan, G., (1970). Chemical nature of the cuticle and its mode of hardening in Eoperipatus weldoni. Acta histochemica 37, 1–17.Google ScholarPubMed
Krishnan, G., & Ravindranath, M. H., (1972). Mode of stabilization of prosclerotin in arthropod cuticles. Acta histochemica (in the Press.)Google ScholarPubMed
Lillie, R. D., (1954). Histopathologic Technic and Practical Histochemistry. New York: Blackiston Company Inc.Google Scholar
Lyons, K. M., (1966). The chemical nature and evolutionary significance of monogenean attachment sclerites. Parasitology 56, 63–100.CrossRefGoogle ScholarPubMed
Monné, L., (1955). On the histochemical properties of the egg envelopes and external cuticles of some parasitic nematodes. Arkives für Zoologie 6, 559–62.Google Scholar
Pearse, A. G. E., (1968). Histochemistry: Theoretical and Applied, vol. 1. London: J. and A. Churchill Ltd.Google Scholar
Ramalingam, K., (1960 a). Comparative and functional morphology of monogenean haptor as revealed in the most advanced types. Proceedings of the National Institute of Sciences of India 26, 352–8.Google Scholar
Ramalingam, K., (1960 b). The functional development of ‘compensating asymmetry’ in the higher monogenea. Zeitschrift für wissenschaftliche Zoologie 164, 374–81.Google Scholar
Ramalingam, K., (1961). A redescription of Lithidiocotyle secunda Tripathi (Monogena) and its bionomics. Journal of Madras University B 31, 143–73.Google Scholar
Ramalingam, K., (1969). Morphological description of Cemocotyleloides gen.n. (Monogenea: Cemocotylidae), its life history and bionomics, pp. 220–41. In Commemoration Volume in Honour of Academician B. E. Bychowsky, pp. 220–41. Zoological Institute, Academy of Sciences, Leningrad, U.S.S.R.Google Scholar
Ramalingam, K., (1971). Studies on vitelline cells of Monogenea. II. Characterization of o-diphenol oxidase. Experimental Parasitology 30, 407–17.CrossRefGoogle ScholarPubMed
Ramalingam, K., (1972). Chemical nature of egg shell of helminths. I. Absence of quinone tanning in the egg shell of liver fluke Fasciola hepatica. International Journal for Parasitology. (In the Press.)Google Scholar
Ramalingam, K., & Ravindranath, M. H., (1971). Differentiation of dihydroxyphenols in biological materials. Acta histochemica 41, 57–61.Google ScholarPubMed
Smyth, J. D., (1954). A technique for the histochemical demonstration of polyphenol oxidase and its application to egg shell formation in helminths and byssus formation in Mytilus. Quarterly Journal of Microscopical Science 95, 139–52.Google Scholar
Smyth, J. D., & Clegg, J. A., (1959). Egg shell formation in trematodes and cestodes. Experimental Parasitology 8, 286–323.CrossRefGoogle ScholarPubMed
Sproston, N. G., (1945). The genus Kuhnia n.g. (Trematode: Monogenea). An examination of the value of some specific characters including factors of relative growth. Parasitology 36, 176–90.CrossRefGoogle Scholar
Sproston, N. G., (1946). A synopsis of monogenetic trematodes. Transactions of Zoological Society, London 25, 185–600.Google Scholar
Weis-Fogh, T., (1960). Resilin: a rubber-like protein. Journal of experimental biology 37, 889–907.CrossRefGoogle Scholar
Weis-Fogh, T., (1963). Resilin, a rubber-like protein and its significance. In Aspects of Protein Structure, (ed. Ramachandran, G. N.), pp. 337–41. New York: Academic Press.Google Scholar
Yamaguti, S., (1963). Systema Helminthum. Vol. 4. Monogenea and Aspidocotylea. New York: Inter-Science Publishers, John Wiley and Sons.Google Scholar