1986
DOI: 10.1017/s0031182000081208
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Amino acid catabolism in the nematodesHeligmosomoides polygyrusandPanagrellus redivivus2. Metabolism of the carbon skeleton

Abstract: All of the enzymes of proline catabolism were present in Heligmosomoides polygyrus and Panagrellus redivivus and the activities were, in general, similar to those found in rat liver. Both nematodes were also shown to be able to catabolize the branched-chain amino acids leucine, isoleucine and valine, by pathways similar to those found in mammalian liver. There were no significant differences in amino acid catabolism between the animal-parasitic and free-living species of nematode.

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Cited by 7 publications
(4 citation statements)
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“…2 e,f). These data are also in good agreement with the findings of analogous intravital experiments 12 .…”
Section: Resultssupporting
confidence: 92%
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“…2 e,f). These data are also in good agreement with the findings of analogous intravital experiments 12 .…”
Section: Resultssupporting
confidence: 92%
“…Besides, a similar pattern of NADPH oxidases activation, i.e. higher in epithelial cells than in cells of the lamina propria, was detected both in explanted duodenum, as presented here, and in the small intestine of living mice 12 . In this way, we validated the experimental model for analyzing the cross-link between host and parasite, along the metabolic axis.…”
Section: Discussionsupporting
confidence: 84%
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“…Up to now, information on metabolism of live parasites (e.g. nematodes) in the host intestine was mostly acquired using bulk biochemical approaches, without spatial or temporal speci cation 9 .…”
Section: Introductionmentioning
confidence: 99%