Tissue specific isozymes of octopine dehydrogenase in the cuttlefish,Sepia officinalis. The roles of octopine dehydrogenase and lactate dehydrogenase inSepia
The activities of octopine dehydrogenase (ODH) and lactate dehydrogenase (LDH) were assayed in the mantle, tentacles, skin, ventricle, branchial heart, ovary, nidamental gland, hepatopancreas, central brain, stellate ganglion, and gill of the cuttlefish,Sepia officinalis. The activities of ODH and LDH are not mutually exclusive; both dehydrogenases were present in each tissue.
LDH was present in heart-type (pyruvate inhibited) and muscle-type forms, the tissue distribution of these two forms being similar to that of the M4 and H4 LDH isozymes of vertebrate tissues.
Cellulose acetate and polyacrylamide gel electrophoresis revealed tissue specific forms of ODH. The enzymes from brain, mantle, and ventricle differ in electrophoretic mobility and several tissues (ex. gill, branchial heart) contain two separable forms of ODH activity.
ODH from hepatopancreas, mantle, brain, and ventricle were characterized kinetically, The brain and hepatopancreas enzymes were found to have the highest affinity for octopine and NAD+. Brain ODH exhibited the lowestKm for arginine and was potently product inhibited by octopine and NAD+.
The role of the ODH/octopine system inSepia appears to be analogous to, but not simply a substitute for, the LDH/lactate system of vertebrates. The possible biological significance of this “double dehydrogenase” system is dicussed.
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- Boucaud-Camou, E.: Localisation d'activités enzymatiques impliquées dans la digestion chezSepia officinalis L. Arch. Zool. exp. gen.115, 5–27 (1974)Google Scholar
- Davis, G.J.: Disc electrophoresis. II. Method and application to human serum protein. Ann. N.Y. Acad. Sci.121, 403–427 (1964)Google Scholar
- Everse, J., Kaplan, N.: Lactate dehydrogenase: Structure and function. Adv. Enzymol.37, 61–148 (1973)Google Scholar
- Fields, J., Baldwin, J., Hochachka, P.W.: On the role of octopine dehydrogenase in cephalopod mantle muscle metabolism. Canad. J. Zool.54, 871–878 (1976a)Google Scholar
- Fields, J., Guderley, H., Storey, K.B., Hochachka, P.W.: The pyruvate branchpoint in squid brain: competition between octopine dehydrogenase and lactate dehydrogenase. Canad. J. Zool.54, 879–885 (1976b)Google Scholar
- Fields, J., Hochachka, P.W.: Octopine dehydrogenase in squid mantle. Comp. Biochem. Physiol.52B, 158 (1975)Google Scholar
- Gäde, G.: Octopine dehydrogenase in the freshwater bivalve,Anodonta cygnea. Comp. Biochem. Physiol.48B, 513–517 (1974)Google Scholar
- Gäde, G., Grieshaber, M.: Partial purification and properties of octopine dehydrogenase and the formation of octopine inAnodonta cygnea L. J. comp. Physiol.102, 149–158 (1975)Google Scholar
- Ghiretti, F.: Respiration. In: Physiology of mollusca, Vol. 2 (eds. K. Wilbur, C. Yonge), pp. 175–208. New York: Academic Press 1966Google Scholar
- Grieshaber, M., Gäde, G.: The biological role of octopine in the squid,Loligo vulgaris L. J. comp. Physiol.103, 225–232 (1976)Google Scholar
- Hiltz, D., Dyer, W.: Octopine in the postmortem adductor muscle of the sea scallop,Placopecten magellanicus. J. Fish. Res. Bd. Canada28, 869–874 (1971)Google Scholar
- Hochachka, P.W., Hartline, P.W., Fields, J.H.A.: Octopine as an end product of anaerobic glycolysis in the chamberedNautilus. Science195, 72 (1977)Google Scholar
- Hochahka, P.W., Moon, T., Mustafa, T., Storey, K.B.: Metabolic sources of power for mantle muscle of a fast swimming squid. Comp. Biochem. Physiol.52B, 151–158 (1975)Google Scholar
- Keely, L.: Characterization of insect fat body mitochondria isolated by a rapid procedure. Comp. Biochem. Physiol.46B, 147–151 (1973)Google Scholar
- Long, G., Kaplan, N.: Lactate dehydrogenase from the horsehoe crab,Limulus polyphemus, and the seaworm,Nereis virens. Arch. Biochem. Biophys.154, 696–710 (1973)Google Scholar
- Moon, T., Hulbert, W.: The ultrastructure of themantle musculature of the squid,Symplectoteuthis oualaniensis. Comp. Biochem. Physiol.52B 145–149 (1975)Google Scholar
- Nauss, K., Davies, R.: Changes in inorganic phosphate and arginine during the development, maintenance, and loss of tension in the anterior byssus retractor muscle ofMytilus edulis. Biochem. Z.345, 173–187 (1966)Google Scholar
- Olomucki, A., Huc, C., Lefebure, F., Thoai, N. van: Octopine dehydrogenase: Evidence for a single chain structure. Europ. J. Biochem.28, 261–268 (1972)Google Scholar
- Poliakov, G.: Neuron structure of the brain, pp. 1–68. Cambridge, Mass: Harvard University Press 1972Google Scholar
- Regnouf, F., Thoai, N. van: Octopine and lactate dehydrogenases in mollusc muscles. Comp. Biochem. Physiol.32, 411–416 (1970)Google Scholar
- Storey, K.B., Hochachka, P.W.: Alpha-glycerophosphate dehydrogenase: its role in the control of the cytoplasmic arm of the alpha-glycerophosphate cycle in squid mantle. Comp. Biochem. Physiol.52B, 169–173 (1975)Google Scholar
- Thoai, N. van, Huc, C., Pho, D., Olomucki, A.: Octopine dehydrogenase: Purification and catalytic properties. Biochim biophys. Acta (Amst.)191, 46–57 (1969)Google Scholar
- Thoai, N. van, Robin, Y.: Metabolisme des derivés guanidyles. VIII. Biosynthèse de l'octopine et repartition de l'enzyme chez les invertebrés. Biochim. biophys. Acta (Amst.)35, 446–453 (1959)Google Scholar
- Thoai, N. van, Robin, Y.: Biochemie comparée des acides amines basiques. Collog. Internat. CNRS92, 353 (1960)Google Scholar
- Williamson, J.R.: Glycolytic control mechanisms. J. biol. Chem.241, 5026–5036 (1966)Google Scholar