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Comparison of glycolytic pentose phosphate pathway glyoxylate shunt krebs cycle enzymes in ganeo tigrinum parasitizing hibernating and nonhibernating rana cyanophlyctis and rana tigrina



Comparison of glycolytic pentose phosphate pathway glyoxylate shunt krebs cycle enzymes in ganeo tigrinum parasitizing hibernating and nonhibernating rana cyanophlyctis and rana tigrina



Journal of Helminthology 57(1): 59-68



The histochemical site and distribution of hexokinase, glycogen phosphorylase (GP Rylase), lactate dehydrogenase (LDH) (key enzymes of glycolysis), glucose-6-phoshate dehydrogenase (GPD) and 6-phosphogluconate dehydrogenase (6PGD) (pentose phosphate shunt enzymes), isocitrate dehydrogenase (IDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH), and .alpha.-ketoglutarate dehydrogenase (.alpha.-KDH) (key enzymes of Krebs' cycle), malate synthetase (MS) and isocitrate lyase (IL) (enzymes of glyoxylate shunt) in various tissues of G. tigrinum from hibernating and nonhibernating R. cyanophlyctis and R. tigrina were studied. Differences in their intensities were revealed. Weak activity of GP Rylase and strong activity of hexokinase in flukes nonhibernating hosts indicates that they utilize glucose through glycolysis for energy turnover. Intense GP Rylase and weak hexokinase activity in worms from hibernating hosts indicates the utilization of glycogen. Strong activity of IDH, SHD, MDH, .alpha.-KGD, MS and IL was demonstrable in the tissues of flukes from nonhibernating hosts; Krebs' cycle and glyoxylate shunt, respectively, may be operating. Tissues of the fluke from hibernating hosts displayed positive activity only for SDH and MDH; no activity for MS and IL, the enzymes of glyoxylate shunt, was observed. Enzymes activities were relatively low in worms from hibernating hosts.

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Accession: 005008192

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