Characterisation of kenyan isolates of plasmodium falciparum by isoenzyme electrophoresis and drug sensitivity.
Abstract
Twenty one Kenyan isolates of Plasmodium falciparum
were characterised by enzyme electrophoresis and
antimalarial drug sensitivity.
For isoenzyme analysis, cellulose acetate and thin
layer starch gel electrophoresis techniques were employed.
P. falciparum isolates from malarious areas of Nyanza, Rift
Valley and Coast provinces were cultivated in vitro and used
in the isoenzyme study. The enzymes of uninfected red blood
cells served as controls.
The enzymes studied were: Glucose phosphate isomerase
(GPI)(EC 5.3.19), 6-phosphogluconate dehydrogenase (6PGD)(EC
1.1.1.44), Lactate dehydrogenase (LDH)(EC 1.1.1.27), NADPdependent
glutamate dehydrogenase (GDH)(EC 1.4.1.4),
Adenosine deaminase (ADA)(EC 3.5.4.4) and Peptidase E
(PEPE)(EC 3.4.11 or 13).
The sensitivitie~ of cultured isolates to seven
antimalarial drugs (chloroquine, amodiaquine, quinine,
quinidine, mefloquine, pyrimethamine and sulphadoxine) were
examined by the in vitro radioisotopic methods of Desjardins
et al.(1979) with minor modifications.
Variant forms of the enzymes GPI and 6PGD were found in
the Kenyan isolates of E. falciparum. GPI enzymes appeared
as GPI-l and GPI-2 variants and 6PGD as 6PGD-l and 6PGD-2
variants. The level of enzyme polymorphism was greater in
Citation
A thesis submitted in partial fulfilment of the requirements for the degree of Master of Science of the University of Nairobi.Publisher
Schooof Science, Chemistry department, University of Nairobi