Caenorhabditis elegans and Ascaris suum: Fragmentation of isocitrate lyase in crude extracts

  • Patel T
  • McFadden B
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Abstract

It is well known that proteolysis often occurs after rupture of metazoan cells. Thus proteins isolated from extracts may not be representative of their native cellular counterparts. In the present research, extensive proteolysis was observed in crude extracts of the freeliving soil nematode Caenorhabditis elegans and the parasitic nematode Ascaris suum. Phenylmethylsulfonyl fluoride (PMSF) reduced the loss in activity of isocitrate lyase (EC 4.1.3.1), fumarase (EC 4.2.1.2), and citrate synthase (EC 4.1.3.7) in extracts of C. elegans but had little or no effect upon loss of malate synthase (EC 4.1.3.2). Catalase (EC 1.11.1.6) was stable. The loss of isocitrate lyase and citrate synthase was less pronounced in extracts of 22-day-old embryos of A. suum. Catalase decayed in these extracts. The addition of PMSF reduced the loss in all three of these activities. Fumarase was stable. The number of active fragments of isocitrate lyase recovered after filtration on Sephadex G-200 increased with the length of storage of crude extracts in the absence of PMSF at 4 C. Even in the presence of PMSF five activity peaks were observed after storage of extracts of C. elegans at 4 C for 72 hr. The molecular weights of active species ranged between 549,000 and 128,000 for isocitrate lyase in extracts of either C. elegans or A. suum. The 549,000- and 214,000-dalton species of isocitrate lyase from A. suum were much more labile at 50 C than the 543,000- and 195,000-dalton species from C. elegans. © 1978.

Author-supplied keywords

  • Ascaris suum, parasitic nematode
  • Caenorhabditis elegans, soil nematode
  • Catalase (EC 1.11.1.6)
  • Citrate synthase (EC 4.1.3.7)
  • Enzymes
  • Escherichia coli, bacterium
  • Fragmentation of isocitrate lyase
  • Fumarase (EC 4.2.1.2)
  • Isocitrate lyase (EC 4.1.3.1)
  • Malate synthase (EC 4.1.3.2)
  • Nematodes
  • Proteolysis in extracts

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Authors

  • Thakor R. Patel

  • Bruce A. McFadden

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