Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0042961 (volvulus)
 4,305 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isozyme analysis was carried out on Onchocerca volvulus worms collected from Liberia, Ivory Coast, Burkina Faso and Sudan to see whether this technique could detect differences between forest and savannah populations of this parasite. A total of 243 forest and 189 savannah individual female worms were electrophoresed and stained for seven enzymes. Four showed some polymorphism, LDH, MDH, PGM and MPI and the other three, GAPDH, PEP and GPI were invariant. Statistical analysis of the results showed that the relative proportions of genotypes from within the different countries conformed to Hardy-Weinberg expectations. Pairwise comparisons of allele frequencies between countries showed that populations from Liberia and Ivory Coast had a very similar composition; there was some divergence between all the other pairs of populations and the genetic distance was calculated to summarize the degree of divergence. The number of loci examined was small and the genetic distances were within the range expected for separate geographical populations of the same species. The usefulness of this technique in worm identification is discussed.
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PMID:Onchocerca volvulus: enzyme polymorphism in relation to the differentiation of forest and savannah strains of this parasite. 302 65

Phosphoglycerate mutase (PGM, EC 5.4.2.1) catalyzes the isomerization of 3-phosphoglycerate and 2-phosphoglycerate in glycolysis and gluconeogenesis. Two distinct types of PGM exist in nature, one that requires 2,3-bisphosphoglycerate as a cofactor (dPGM) and another that does not (iPGM). The two enzymes are structurally distinct and possess different mechanisms of action. In any particular organism, one form may exist or both. Nematodes possess the iPGM form whereas mammals have dPGM. In the present study, we have cloned and expressed iPGM from Onchocerca volvulus and described the catalytic properties of O. volvulus, Brugia malayi and Caenorhabditis elegans iPGM enzymes. Temperature and pH optima were determined for each enzyme. Like other iPGM enzymes, the activities of the nematode iPGM enzymes were dependent on the presence of divalent ions. Inactivation by EDTA could be restored most effectively by magnesium and manganese ions. Kinetic parameters and specific activities of the various recombinant enzymes were determined. The high similarity in catalytic properties among the enzymes indicates that a single enzyme inhibitor would likely be effective against all nematode enzymes. Inhibition of iPGM activity in vivo may lead to lethality as indicated by RNAi studies in C. elegans. Our results support the development of iPGM as a promising drug target in parasitic nematodes.
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PMID:Molecular and biochemical characterization of nematode cofactor independent phosphoglycerate mutases. 1789 34