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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
- Source :
- Molecular and Biochemical Parasitology. 23:25-29
- Publication Year :
- 1987
- Publisher :
- Elsevier BV, 1987.
-
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.
- Subjects :
- Echinococcosis, Hepatic
UTP-Glucose-1-Phosphate Uridylyltransferase
Cestoda
Uridine Triphosphate
Biology
Echinococcus multilocularis
Chromatography, Affinity
Affinity chromatography
medicine
Animals
Transferase
Parasite hosting
Cyst
Molecular Biology
chemistry.chemical_classification
UTP—glucose-1-phosphate uridylyltransferase
Glucosephosphates
biology.organism_classification
medicine.disease
Nucleotidyltransferases
Molecular biology
Echinococcus
Kinetics
Enzyme
Liver
Biochemistry
chemistry
Parasitology
Gerbillinae
Subjects
Details
- ISSN :
- 01666851
- Volume :
- 23
- Database :
- OpenAIRE
- Journal :
- Molecular and Biochemical Parasitology
- Accession number :
- edsair.doi.dedup.....efe4a5a3e4e167282250b67019c47ce4
- Full Text :
- https://doi.org/10.1016/0166-6851(87)90183-6