A comparative study of UTP-D-glucose-1-phosphate uridylyl transferase in the cysts of Echinococcus multilocularis and the livers of infected and control Meriones unguiculatus.

Abstract

Kinetic and physical parameters of UDP-glucose pyrophosphorylase were determined in Meriones unguiculatus infected with Echinococcus multilocularis metacestodes (cestoda). Studies were carried out on parasite cysts, and on livers from control and infected animals after purification of the enzyme by affinity chromatography on UTP-agarose. The enzyme from infected and control livers had km values for UTP of 0.01 mM and 0.5 mM, respectively; for glucose-1-phosphate values were 0.46 mM and 0.07 mM, respectively. On the other hand the enzyme from cysts was found to have a higher Km for UTP (1 mM) and for glucose-1-phosphate (1.5 mM) than from infected or non-infected livers. Physical characteristics (pI = 6 and Mr = 160,000) of UDP-glucopyrophosphorylases were the same in controls and infected host livers but were different from the cyst enzyme (pI = 7 and Mr = 251,000). These results provide evidence for the existence of significant differences between parasitic and host enzymes, which could possibly be exploited in chemotherapy.

• Authors: M E Sarciron, G Azzar, F Persat, A F Petavy, R Got
• Journal: Molecular and biochemical parasitology (Mol Biochem Parasitol) Vol. 23 Issue 1 Pg. 25-9 (Feb 1987) ISSN: 0166-6851 [Print] Netherlands
• PMID: 3033498 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Glucosephosphates
• glucose-1-phosphate
• Nucleotidyltransferases
• UTP-Glucose-1-Phosphate Uridylyltransferase
• Uridine Triphosphate

Topics

• Animals
• Chromatography, Affinity
• Echinococcosis, Hepatic (enzymology)
• Echinococcus (enzymology)
• Gerbillinae (parasitology)
• Glucosephosphates (metabolism)
• Kinetics
• Liver (enzymology)
• Nucleotidyltransferases (metabolism)
• UTP-Glucose-1-Phosphate Uridylyltransferase (metabolism)
• Uridine Triphosphate (metabolism)