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Moniezia expansa

Barrett, J., Saghir, N., Timanova, A., Clarke, K and Brophy, P.M. (1997) Characterisation and properties of an intracellular lipid-binding protein from the tapeworm Moniezia expansa. European Journal of Biochemistry 250, 269-275. [Pg.333]

Janssen, D. and Barrett, J. (1995) A novel lipid-binding protein from the cestode Moniezia expansa. BiochemicalJournal ill, 49—57. [Pg.334]

P. G. C. Douch, H. M. Gahagan, The Metabolism of Niclosamine and Related Compounds by Moniezia expansa, Ascaris lumbricoides var suum, and Mouse and Sheep-Liver Enzymes , Xenobiotica 1977, 7, 301-307. [Pg.175]

Elliott, D.C.V. (1986) Tapeworm (Moniezia expansa) and its effect on sheep production the evidence reviewed. New Zealand Veterinary Journal 34, 61-65. [Pg.252]

Southworth, J., Harvey, C. and Larson, S. (1996) Use of praziquantel for the control of Moniezia expansa in lambs. New Zealand Veterinary Journal 44, 112-115. [Pg.254]

Arthurdendyus triangulatus NPF Moniezia expansa NPF Schistosoma japonicum NPF Schistosoma mansoni NPF Aplysia californica NPF Lymnaea stagnalis NPF Drosophila melanogaster NPF Lamprey NPY Homo sapiens NPY... [Pg.377]

Mair, G.R., Halton, D.W., Shaw, C. and Maule, A.G. (2000) The neuropeptide F (NPF) encoding gene from the cestode, Moniezia expansa. Parasitology 120, 71-77. [Pg.384]

Miskolzie, M. and Kotovych, G. (2002) The NMR-derived conformation of neuropeptide F from Moniezia expansa. Journal of Biomolecular Structure and Dynamics 19, 991 -998. [Pg.385]

The major phosphagens found in nature are arginine and creatine but parasitic helminths are unusual in that they possess no detectable phosphagens and none occurs in Hymenolepis diminuta, Moniezia expansa, Ligula intestinalis or Schistocephalus solidus (44). This absence of phosphagens has implications for control of metabolism in cestodes. If... [Pg.63]

Some recent studies include those on Cotugnia digonopora and Raillietina fuhrmanni (595, 596, 597) R. cesticillus (635) R. tetragona and R. echinobothrida (915,917) Hymenolepis diminuta(37,371) Echinococcus granulosus (231,341,522, 685) Taenia taeniaeformis (537-539) Taenia crassiceps (540) Moniezia expansa... [Pg.65]

Fig. 4.4. HPLC fractionation of the free ecdysteroid fraction from Moniezia expansa (a) sample 1, 3.3% portion (bj sample 2, 10% portion on a chromatographic system with collection of fractions every minute for the radioimmunoassay (RIA) (ICT-1 antiserum). The positions of authentic ecdysteroids are shown IV, 20, 26-dihydroxyecdysone II, 20-hydroxyecdysone I, ecdysone. (After Mendis et al., 1984.)... Fig. 4.4. HPLC fractionation of the free ecdysteroid fraction from Moniezia expansa (a) sample 1, 3.3% portion (bj sample 2, 10% portion on a chromatographic system with collection of fractions every minute for the radioimmunoassay (RIA) (ICT-1 antiserum). The positions of authentic ecdysteroids are shown IV, 20, 26-dihydroxyecdysone II, 20-hydroxyecdysone I, ecdysone. (After Mendis et al., 1984.)...
Moniezia expansa (Adult) Lactate, succinate Similar to aerobic with... [Pg.84]

This enzyme catalyses the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate (FBP) and is the key regulatory enzyme of glycolysis. The properties of phosphofructokinase (PFK) have been investigated in some detail in adult Moniezia expansa (60) and in plerocercoids of S. solidus (65), where its activity is modulated by a number of compounds, including ATP, AMP, fructose-6-phos-phate, Mg2 +, Mn2 +, K + and NH. In general, the PFKs from both species exhibit properties similar to those of the enzymes from mammalian sources and they probably regulate glycolysis in the same manner as their mammalian counterparts. The inhibitory effects of ATP on the PFK from Schistocephalus solidus and the relief of this inhibition by AMP are shown in Fig. 5.2. [Pg.88]

It is not possible to generalise on the control of the PEP branchpoint in cestodes because different metabolites can act as modulators of pyruvate kinase and PEPCK in different species. The branchpoint has been most studied in Moniezia expansa (59,61,98,103) and in H. diminuta (568,612, 650). [Pg.94]

Fig. 5.5. Proposed pathways of metabolism in Moniezia expansa scoleces under aerobic conditions cytosolic reactions. (After Bryant Behm, 1976.) OAA, oxaloacetate PYR, pyruvate, MAL, malate, LACT, lactate for other abbreviations, see the text. Fig. 5.5. Proposed pathways of metabolism in Moniezia expansa scoleces under aerobic conditions cytosolic reactions. (After Bryant Behm, 1976.) OAA, oxaloacetate PYR, pyruvate, MAL, malate, LACT, lactate for other abbreviations, see the text.
It has been purified (445) and shares some properties in common with malic enzymes from mammals and birds in being NADP-dependent, heat-stable and able to decarboxylate oxaloacetate. The malic enzyme of H. microstoma also has a marked specificity for NADP (216), contrasting with that of Spirometra mansonoides, which appears to be both NAD- and NADP-linked (220). Malic enzyme has been demonstrated in a range of other cestodes including Mesocestoides corti (399), Schistocephalus solidus (406), Moniezia expansa (60), Echinococcus spp. (500) and L. intestinalis (502). [Pg.99]

The electron transport system of cestodes has been comprehensively reviewed by Cheah (129) earlier reviews are those by Smyth (796) and Bryant (97). To date, only the electron transport systems of large intestinal cestodes - Moniezia expansa, Taenia hydatigena, T. taeniaeformis, H. diminuta -have been investigated in detail. The mitochondria of such cestodes have structural characteristics similar to those present in mammalian tissues (25, 298), although variation in number, form and size has been noted in different strobilar regions such as the tegument, parenchyma and reproductive tissue (455). [Pg.107]

Fig. 5.11. Proposed electron transport system of Moniezia expansa. (After Cheah, 1983.)... Fig. 5.11. Proposed electron transport system of Moniezia expansa. (After Cheah, 1983.)...
Proteolytic activity has also been detected in Schistocephalus solidus (777), Ligula intestinalis (514, 515,516), Taenia saginata (287, 288), Moniezia expansa (182) and E. granulosus (491). [Pg.132]

Behm, C. A. Bryant, C. (1975a). Studies of regulatory metabolism in Moniezia expansa general conditions. International Journal for Parasitology, 5 209-17. [Pg.309]

Metabolic regulation in Moniezia expansa (Cestoda) the role of pyruvate kinase. International Journalfor Parasitology, 2 333— 40. [Pg.311]

Bryant, C. Behm, C. A. (1976). Regulation of respiratory metabolism in Moniezia expansa under aerobic and anaerobic conditions. In Biochemistry of parasites and host-parasite relationships, ed. H. Van den Bossche, pp. 89-94. North-Holland Publishing Co. Amsterdam. [Pg.311]

Cheah, K. S. (1967a). The oxidase systems of Moniezia expansa (Cestoda). Comparative Biochemistry and Physiology, 23 277-302. [Pg.312]


See other pages where Moniezia expansa is mentioned: [Pg.244]    [Pg.375]    [Pg.377]    [Pg.55]    [Pg.56]    [Pg.57]    [Pg.63]    [Pg.68]    [Pg.93]    [Pg.94]    [Pg.94]    [Pg.105]    [Pg.108]    [Pg.108]    [Pg.108]    [Pg.111]    [Pg.123]    [Pg.148]    [Pg.159]    [Pg.175]    [Pg.242]    [Pg.309]    [Pg.309]   
See also in sourсe #XX -- [ Pg.22 , Pg.129 , Pg.281 ]

See also in sourсe #XX -- [ Pg.65 ]




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