Da. Johnston et Ma. Fernando, ISOENZYMES OF EIMERIA FROM THE DOMESTIC-FOWL - ELECTROPHORETIC VARIANTS AMONG SPECIES, STRAINS AND CLONES, Parasitology research, 83(5), 1997, pp. 464-470
Electrophoretic variation of enzymes in five Eimeria spp. of the domes
tic fowl, including nine strains, ten single-sporocyst clones and two
single-sporozoite clones of E. acervulina, three strains each of E. ma
xima and E. tenella, two strains of E. praecox and one strain of E. ne
catrix, were assayed using cellulose acetate electrophoresis. Ten enzy
mes [aldehyde oxidase (AO), alkaline phosphatase (ALP), amylase (AMY),
fumarate hydratase (FUM), glucose-6-phosphate dehydrogenase (G6PDH),
glucose phosphate isomerase (GPI), glutamate-oxaloacetate transferase
(GOT), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH) and
phosphoglucomutase (PGM)] were analyzed for their ability to distingui
sh between these species and strains. Enzymatic activity of G6PDH, GPI
, IDH, MDH and PGM was detected in all the Eimeria spp. examined. Stra
ins within each species were characterized by the same electrophoretic
variant of G6PDH. Electrophoretic variants of GPI and PGM were the mo
st valuable in the identification of inter- and intra-specific variati
on, particularly in the field strains of E. acervulina and E. tenella.
These two enzymes were used to examine single-sporocyst and single-sp
orozoite clones derived from two strains of E. acervulina. The enzymes
in E. maxima appeared to be conserved, showing no variation among str
ains with the five enzymes detected. Relative mobilities, calculated a
s described in this paper, were found to be consistent between differe
nt electrophoresis runs and may serve as a reference when this medium
is used.