Glucose-6-phosphate dehydrogenase and malate dehydrogenase enzyme electrophoretic patterns amongst strains of Bacteroides fragilis.
Fifty-two strains of Bacteroides fragilis were examined for their enzyme electrophoretic patterns of glucose-6-phosphate dehydrogenase (G6PDH) and malate dehydrogenase (MDH). All strains tested possessed high levels of both enzymes but the G6PDH reduced NADP whereas MDH was NAD-dependent. Twenty-seven strains produced single bands of both G6PDH and MDH. In all cases G6PDH migrated faster than MDH. Strains clustered by a single linkage algorithm were recovered in eight clusters at the 77% similarity level. The remaining 25 strains produced multiple bands of one or both enzymes. These were recovered in six clusters at the 72% similarity level using the same algorithm. The results of this study revealed considerable heterogeneity of enzyme patterns within B. fragilis.
Shah
H N
HN
Department of Microbiology, Faculty of Medicine, Kuwait University.
Al-Jalili
T A
TA
Elhag
K M
KM
Mundegar
Z R
ZR
D001441:Bacteroides fragilis / Q000145:classification / Q000201:enzymology*; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D006801:Humans; D008291:Malate Dehydrogenase / Q000378:metabolism*
D008291:Malate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase