Biochemical studies on cysticercus fasclclaris: demonstration of certain hydrolytic and oxidative enzymes and isoenzymes, 1983
Ndifor, Fombotioh
1980-1989
Biochemical studies were carried out on fresh whole worm extracts of Cysticercus fasciolaris in order to demonstrate certain enzyme systems. Acid phosphatase (AcP), alkaline phosphatase (A1P), acetylcholinesterase (AChE), creatine phosphokinase (CPK), lactate dehydrogenase (LDH), and malate dehydrogenase (MDH) were determined quantitatively and demonstrated spectrophotometrically. Similar studies were conducted on the sera of the host. All the enzymes studied were found to be present in sera of infected and noninfected rats; however, the infected animals showed significantly higher levels of CPK, LDH and MDH. Changes involving the activities of AcP, A1P and AChE were insignificant. Elevations in levels of certain specific enzymes in sera of infected animals were attributed to the presence of C^. fasciolaris. Polyacrylamide gel electrophoresis was used to study isoenzymes and protein bands in fresh whole worm extracts and liver tissue homogenates in infected and uninfected rats. Isoenzymes for 6-phosphoglu-conate dehydrogenase (6-PGDH), glucose-6-phosphate dehydrogenase (G-6-PDH), a-glycerophosphate dehydrogenase (a-GPDH), lactate dehydrogenase iii(LDH), malate dehydrogenase (MDH), isocitrate dehydrogenase (ICDH), succinate dehydrogenase (SDH), glutamate dehydrogenase (GLDH), g-hydroxy-butyrate dehydrogenase (0-HBDH), NADH diaphorase (NADHD), and NADPH diaphorase (NADphd) were demonstrated. Hydrolytic isoenzymes of nonspecific esterases (NSE), acid phosphatase (AcP) and alkaline phosphatase (A1P) were also demonstrated. Alcohol dehydrogenase (ALDH) was not detected in worm extracts, but was present in liver tissues homogenates of both uninfected and infected rats. It is suggested that significant alcoholic fermentation does not occur in C_. fasciolaris since ALDH is not present. The presence of Ct-GPDH and LDH suggests a typical glycolytic pathway. Krebs citric acid cycle is indicated because of the presence of 6-PGDH and G-6-PDH. The presence of NADHD and NADphd in C_. fasciolaris suggests that the electron transport system operates in this organism. There were some significant variations in the number and pattern of isoenzymes in the parasite and in the liver homogenates of infected and uninfected animals. Molecular variations were observed between enzymes of C_. fasciolaris and similar enzymes in the intermediate host. The knowledge derived from this research could possibly be useful in the diagnosis of human cysticercosis by an evaluation of the presence of isoenzymes in the sera of infected hosts.
text
application/pdf
1983-12-01
dissertation
Doctor of Philosophy (PhD)
Atlanta University
Department of Biology
LeFlore, W. B.
Clark Atlanta University
Georgia--Atlanta
http://hdl.handle.net/20.500.12322/cau.td:1983_ndifor_fombotioh