5′-Nucleotidase activity and substrate affinity in digenetic trematodes
- 1 September 1985
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Helminthology
- Vol. 59 (3) , 263-266
- https://doi.org/10.1017/s0022149x00008063
Abstract
5′-nucleotidases of eight species of digenetic trematodes were studied using five different substrates. All species showed the following preferential order of substrate affinity; AMP>CMP>GMP>TMP>UMP. It was observed that different species occupying similar habitats possessed closely related levels of enzyme activities. The function of 5′-nucleotidases in trematodes is also suggested.Keywords
This publication has 6 references indexed in Scilit:
- Non-specific alkaline phosphomonoesterases of eight species of digenetic trematodesJournal of Helminthology, 1975
- Megalodiscus temperatus: Absorption and incorporation of tritiated tyrosine, thymidine, and adenosineExperimental Parasitology, 1974
- 5′-NucleotidasePublished by Elsevier ,1974
- Gorgoderina attenuata: Uptake and incorporation of tyrosine, thymidine, and adenosineExperimental Parasitology, 1973
- Pathways of nucleotide metabolism in Schistosoma mansoni—II: Disposition of adenosine by whole wormsBiochemical Pharmacology, 1973
- Chromatographic separation, identification, and analysis of phosphatidesJournal of Lipid Research, 1962