Results 111 to 120 of about 549 (156)

The oxidase systems of Moniezia expansa (Cestoda)

Comparative Biochemistry and Physiology, 1967
1. 1. Moniezia expansa has a branched respiratory chain system with two terminal oxidases, cytochrome oxidase and an o-type cytochrome. 2. 2. The major pathway involving the o-type pigment tentatively designated “Cytochrome 552, 556 (Moniezia expansa)” (77°K), the major terminal oxidase, is shown to be closely associated with fumarate reduction ...
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l-Lysine carboxylyase in Ascaris lumbricoides and Moniezia expansa

Experimental Parasitology, 1968
Abstract Homogenates of Ascaris lumbricoides var. suis of Moniezia expansa show remarkable l -lysine decarboxylase activity. Optimun pH is 4.8 and 5.0, respectively. In preliminary treatment with DEAE-cellulose a single fraction possessing activity was obtained, but when the extracts were submitted to electrophoresis at pH 8.6 there were two active ...
J, López-Gorgé, M, Monteoliva, F, Mayor   +2 more
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The Life-Cycle of Moniezia expansa

The Journal of Parasitology, 1932
Recent publications on the life-history of the Anoplocephalid tapeworms of sheep (Konsuloff, I929, Monnig, I929, Sinitsin, 1931, Scott & Honess, 1931) encourage the writer in the belief that a brief survey of the literature, together with records of certain experiments carried out in England in 1923, may be of interest to workers engaged in the study ...
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The purification and properties of glutathione reductase from the cestode Moniezia expansa

The International Journal of Biochemistry & Cell Biology, 1995
Glutathione reductase has a central role in glutathione metabolism and as such is a potential target for chemotherapy. The aim of the work was to purify and characterise glutathione reductase from the cestode Moniezia expansa and to compare the properties of the helminth enzyme with its mammalian counterpart. The enzyme was purified by a combination of
M J, McCallum, J, Barrett
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Studies of regulatory metabolism in Moniezia expansa: The role of phosphoenolpyruvate carboxykinase

International Journal for Parasitology, 1975
Abstract Phosphoenolpyruvate carboxykinase (PEPCK) from M. expansa has been partially purified and its behaviour in a range of different assay conditions has been determined. Different PEPCK's were found in the cytosol and mitochondria. Some kinetic parameters for each are presented.
C A, Behm, C, Bryant
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Infectivity of Moniezia benedeni and Monieza expansa to oribatid mites from Ohio and Georgia

Veterinary Parasitology, 1992
Six species of oribatid mites belonging to four families and five genera were successfully infected by M. benedeni. They were Scheloribates laevigatus (Scheloribatidae), Exoribatula sp. cf. biundatus (Scheloribatidae), Xylobates capucinus (Haplozetidae) and Zygoribatula undulata (Oribatulidae) from Ohio, and Galumna ithacensis (Galumnidae) and ...
L, Xiao, R P, Herd
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The tricarboxylic acid cycle and associated reactions in Moniezia expansa (Cestoda)

Comparative Biochemistry and Physiology, 1969
Abstract 1. 1. Experiments with radioactive substrates have provided evidence for the presence of the tricarboxylic acid cycle in Moniezia expansa . 2. 2. Incorporation of 14 CO 2 probably involves both “malic enzyme” and phosphoenol pyruvate carboxykinase.
R A, Davey, C, Bryant
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Moniezia benedeni and Moniezia expansa are distinct cestode species based on complete mitochondrial genomes

Acta Tropica, 2017
Moniezia spp. parasitize the intestines of ruminants, causing monieziasis. In this study, the complete mitochondrial (mt) genomes of M. benedeni and M. expansa have been determined, characterized and employed to test the hypothesis that M. benedeni and M.
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Studies on the electron transport system of Moniezia expansa (CESTODA)

Comparative Biochemistry and Physiology, 1966
Abstract 1. 1. Succinoxidase and NADH oxidase systems in a particulate fraction from Moniezia expansa were studied by manometric and spectrophotometric methods. 2. 2. The use of redox dyes and inhibitors showed that succinate and NADH oxidation were accomplished by mechanisms which differed from those in mammalian tissues. 3. 3. Succinate
K.S. Cheah, C. Bryant
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Peroxide metabolism in the cestodes Hymenolepis diminuta and Moniezia expansa

International Journal for Parasitology, 1980
Abstract The enzymes of hydrogen peroxide metabolism have been investigated in the cestodes H. diminuta and M. expansa . Neither catalase, lipoxygenase, glutathione peroxidase, NADH peroxidase nor NADPH peroxidase could be detected in homogenates of either species. However, both H. diminuta and M.
J.M. Paul, J. Barrett
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