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Preliminary studies on haemoglobin and other proteins of the Pogonophora

Published online by Cambridge University Press:  11 May 2009

Clyde Manwell ,
E. C. Southward  and
A. J. Southward
Clyde Manwell
Affiliation:
The Plymouth Laboratory
E. C. Southward
Affiliation:
The Plymouth Laboratory
A. J. Southward
Affiliation:
The Plymouth Laboratory
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Extract

Starch gel electrophoresis of extracts of Siboglinum atlanticum showed that all five individuals tested have two acidic haemoglobin components and a strong α-naphthyl acetate esterase. There was individual variation in the position of the esterase. Low levels of amylase activity were found in the extracts but no trace of dehydrogenases for such important substrates as glucose-6-phosphate, lactate, malate, and glutamate could be revealed by standard histochemical methods as applied to zone electrophoresis. The high level of haemoglobin and the protein peculiarities of the Pogonophora are discussed in relation to experiments on respiration. It is concluded that Siboglinum haemoglobin functions at very low oxygen partial pressures and that the high level of haemoglobin dissolved in the blood plasma of pogonophores does not reflect a high level of oxygen consumption or activity. The meagre biochemical data at present available on the Pogonophora do not favour relationship of this phylum to the echinodtrm-chordate line any more than to the annelids or other invertebrate phyla.

INTRODUCTION

Largely as a result of studies by A. V. Ivanov, the phylum Pogonophora has become recognized by zoologists in the past decade (reviewed by Hyman, 1959, esp. pp. 208–27; Ivanov, 1963; E. C. Southward, 1963). Pogonophores are small, extremely vermiform animals, living in tubes partly im-bedded in mud or muddy sand; while in some areas they are sufficiently abundant to dominate the benthic fauna, their occurrence at great depths has made living pogonophores very difficult to obtain.

Two especially interesting problems associated with this newly recognized phylum are:(a) Pogonophora are the only group of free-living Metazoa without a gut at any stage in their development, and thus, the method of feeding and type of metabolism has been the subject of considerable speculation; (b) Pogonophora possess a few characteristics—e.g. a ventral heart and dorsal nerve cord—suggestive of the echinoderm-chordate line of evolution.

Type
Research Article
Information
Journal of the Marine Biological Association of the United Kingdom , Volume 46 , Issue 1 , February 1966 , pp. 115 - 124
Copyright
Copyright © Marine Biological Association of the United Kingdom 1966

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References

REFERENCES

Allen, S. L., 1961. Genetic control of the esterases in the protozoan Tetrahymena pyriformis. Ann. N.Y. Acad. Sci., Vol. 94, pp. 735–73.CrossRefGoogle ScholarPubMed
Baker, C. M. A., Manwell, C., Labisky, R. & Harper, J., 1965. Molecular genetics of avian proteins. V. Egg, blood and tissue proteins of the Ring-necked Pheasant, Phasianus colchicus L. Comp. Biochem. Physiol. (in the Press).CrossRefGoogle Scholar
Beckman, L. & Johnson, F. M., 1964. Esterase variations in Drosophila melanogaster. Hereditas, Vol. 51, Pp. 212–22.CrossRefGoogle Scholar
Brunet, P. C. J. & Carlisle, D. B., 1958. Chitin in Pogonophora. Nature, Lond., Vol. 182, p. 1689.CrossRefGoogle Scholar
Ferguson, K. A. & Wallace, A. L. C, 1961. Starch gel electrophoresis of anterior pituitary hormones. Nature, Lond., Vol. 190, pp. 629–30.CrossRefGoogle ScholarPubMed
Fox, H. M. & Wingfield, C. A., 1938. A portable apparatus for the determination of oxygen dissolved in a small volume of water. J. exp. Biol., Vol. 15, pp. 437–45.CrossRefGoogle Scholar
Goldberg, E. & Cather, J. N., 1963. Molecular heterogeneity of lactic dehydrogenase during development of the snail Argobuccinum oregonense Redfield. J. cell. comp. Physiol., Vol. 61, pp. 31–8.CrossRefGoogle Scholar
Hogben, L., 1946. An Introduction to Mathematical Genetics. New York: W. W. Norton and Co.Google Scholar
Hyman, L. H., 1959. Smaller coelomate groups. The Invertebrates, Vol. V. New York: McGraw-Hill Book Company.Google Scholar
Ivanov, A. V., 1963. Pogonophora(translated by Carlisle, D. B.). London: Academic Press.CrossRefGoogle Scholar
Johnson, F. H., Eyring, H. & Pollisar, M. J., 1954. The Kinetic Basis of Molecular Biology. New York: John Wiley.Google Scholar
Kaplan, N. O., 1963. Symposium on multiple forms of enzymes and control mechanisms. I. Multiple forms of enzymes. Bact. Rev., Vol. 27, pp. 155–69.CrossRefGoogle ScholarPubMed
Kaplan, N. O., Ciotti, M. M., Hamolsky, M. & Bieber, R. E., 1960. Molecular heterogeneity and evolution of enzymes. Science, N.S., Vol. 131, pp. 392–7.CrossRefGoogle ScholarPubMed
Latner, A. L. & Skillen, A. W., 1961. Clinical applications of dehydrogenase isoenzymes. Lancet, 1961, Vol. 2, pp. 1286–8.CrossRefGoogle ScholarPubMed
Manwell, C., 1958. On the evolution of hemoglobin. Respiratory properties of the hemoglobin of the California Hagfish, Polistotrema stoutii. Biol. Bull. mar. biol. Lab., Woods Hole, Vol. 115, pp. 227–38.CrossRefGoogle Scholar
Manwell, C, 1959. Alkali denaturation and oxygen equilibrium of annelid hemoglobins. J. cell. comp. Physiol., Vol. 53, pp. 61–74.CrossRefGoogle Scholar
Manwell, C., 1960a. Comparative physiology; blood pigments. A. Rev. Physiol., Vol. 22, pp. 191–244.CrossRefGoogle ScholarPubMed
Manwell, C., 1960b.Oxygen equilibrium of brachiopod Lingula hemerythrin Science, N.S., Vol. 132, pp. 550–1.Google Scholar
Manwell, C., 1960c. Histological specificity of respiratory pigments. I. Comparisons of the coelom and muscle hemoglobins of the polychaete worm Travisia pupa and the echiuroid worm Arhynchite pugettensis. Comp. Biochem. Physiol, Vol. 1, pp. 267–76.CrossRefGoogle Scholar
Manwell, C., 1963. The blood proteins of cyclostomes: a study in phylogenetic and cntogenetic biochemistry. In The Biology of Myxine, pp. 372–455. (Brodal, A. & Fange, R., editors), Universitetsforlaget, Oslo.Google Scholar
Manwell, C., 1964. Chemistry, genetics, and function of invertebrate respiratory pigments—configurational changes and allosteric effects. In Oxygen in the Animal Organism, I.U.B. Symposium Series, Vol. 31, pp. 49–119. (Dickens, F. & Neil, E., editors). Oxford: Pergamon Press.CrossRefGoogle Scholar
Manwell, C., 1965. Metamorphosis and gene action. I. Electrophoresis of dehydrogenases, esterases, phosphatases, hemoglobins, and other soluble proteins of tadpole and and adult bull frogs. Comp. Biochem. Physiol. (in the Press).CrossRefGoogle Scholar
Manwell, C. & Baker, C. M. A., 1963a. A sibling species of sea cucumber discovered by starch gel electrophoresis. Comp. Biochem. Physiol., Vol. 10, pp. 39–53.CrossRefGoogle ScholarPubMed
Manwell, C. & Baker, C. M. A. 1963b. Starch gel electrophoresis of sera from marine arthropods: studies on the heterogeneity of hemocyanin and on a ‘ ceruloplasmin-like protein’. Comp. Biochem. Physiol., Vol. 8, pp. 193–208.CrossRefGoogle Scholar
Markert, C., & Hunter, R. L., 1959. The distribution of esterases in mouse tissues. J. Histochem. Cytochem., Vol. 7, pp. 42–9.CrossRefGoogle ScholarPubMed
Manwell, C. & Kerst, K. V., 1965. Possibilities of biochemical taxonomy of bats using hemoglobin, lactate dehydrogenase, esterases and other proteins. Comp. Biochem. Physiol. (in the Press).CrossRefGoogle Scholar
Markert, C. & Moller, F., 1959. Multiple forms of enzymes: tissue, ontogenetic, and species specific patterns. Proc. natn. Acad. Sci. U.S.A., Vol. 45, pp. 753–63.CrossRefGoogle ScholarPubMed
Moore, R. O.& Villee, C. A., 1963. Multiple molecular forms of malate dehydrogenase in echinoderm embryos. Comp. Biochem. Physiol. Vol. 9, pp. 81–94.CrossRefGoogle Scholar
Popp, R. A., 1961. Inheritance of different serum esterase patterns among inbred strains of mice. Genetics, Princeton, Vol. 46, p. 890.Google Scholar
Scholander, P. F., Flagg, W., Walters, V. & Irving, L. 1953. Climatic adaptation in arctic and tropical poikilotherms. Physiol. Zodl., Vol. 26, pp. 67–92.Google Scholar
Schwartz, D., 1950. Genetic studies on mutant enzymes in maize: synthesis of hybrid enzymes by heterozygotes. Proc. natn. Acad. Sci. U.S.A., Vol. 46, p. 1210–15.CrossRefGoogle Scholar
Southward, A. J. & Crisp, D. J., 1965. Activity rhythms of barnacles in relation to respiration and feeding. J. mar. biol. Ass. U.K., Vol. 45, pp. 161–85.CrossRefGoogle Scholar
Southward, A. J. & Southward, E. C, 1963. Notes on the biology of some Pogonophora. J. mar. biol. Ass. U.K., Vol. 43, pp. 57–64.CrossRefGoogle Scholar
Southward, E. C, 1963. Pogonophora. Oceanogr. mar. BioL, A. Rev., Vol. 1, pp. 405–28.Google Scholar
Southward, E. C. & Southward, A. J., 1966. A preliminary study of the general and enzyme histochemistry of some Pogonophora. (in preparation).Google Scholar
Tsao, M. U., 1960. Heterogeneity of tissue dehydrogenases. Archs Biochem. Biophys., Vol. 90, pp. 234–8.CrossRefGoogle ScholarPubMed
Vesell, E. S. & Philip, J., 1963. Application of multiple molecular forms of enzymes in biology. In Protides of the Biological Fluids (Peeters, H., editor), Vol. 10, pp. 28–40. Amsterdam: Elsevier Publishing Company.Google Scholar
Wilson, A. C, Cahn, R. D. & Kaplan, N. O., 1963. The functions of the two forms of lactic dehydrogenase in the breast muscle of birds. Nature, Lond., Vol. 197, PP. 331–4.CrossRefGoogle ScholarPubMed
Wilson, A. C. & Kaplan, N. O., 1964. Enzyme structure in its relation to taxonomy. In Taxonomic Biochemistry and Serology (Leone, C. A., editor), pp. 321–46. New York: Ronald Press.Google Scholar
Wright, T. R. F., 1963. The genetics of an esterase in Drosophila melanogaster. Genetics, Princeton, Vol. 48, pp. 787–801.CrossRefGoogle ScholarPubMed
Zeuthen, E., 1947. Body size and metabolic rate in the animal kingdom. C. r. Trav. Lab. Carlsberg, Ser. Chim., Vol. 26, pp. 17–161.Google Scholar