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3.
Comp Biochem Physiol B ; 93(4): 789-92, 1989.
Article in English | MEDLINE | ID: mdl-2553330

ABSTRACT

1. This paper reports the isolation and the partial purification of cAMP phosphodiesterase (EC 3.1.4.17) from the promastigote form of Leishmania tropica and a preliminary result from Leishmania donovani. 2. The activity of the fraction obtained from column chromatography was measured. 3. The effects of pH, temperature, time of incubation and various compounds on its activity in vitro were obtained. 4. Two peaks (I and II) exhibiting cyclic nucleotide phosphodiesterase activity were obtained. 5. Both activities were found to require the addition of Mg2+ ions for full effect. 6. The apparent Km values for the first and second peaks were 1.43 x 10(-3) M and 4.1 x 10(-3) M respectively. L. donovani shows only one peak of activity.


Subject(s)
3',5'-Cyclic-AMP Phosphodiesterases/isolation & purification , Leishmania donovani/enzymology , Leishmania tropica/enzymology , 3',5'-Cyclic-AMP Phosphodiesterases/metabolism , Animals , Caffeine/pharmacology , Calcium/pharmacology , Hydrogen-Ion Concentration , Kinetics , Magnesium/pharmacology , Phenobarbital/pharmacology , Substrate Specificity , Temperature , Theophylline/pharmacology , Trifluoperazine/pharmacology
4.
Environ Pollut ; 57(4): 281-7, 1989.
Article in English | MEDLINE | ID: mdl-15092442

ABSTRACT

The effects of four lindane concentrations, i.e. 20, 40, 60 and 80 microg ml(-1), on the nucleic acid, protein and carbohydrate content of Tetrahymena pyriformis have been examined. All the test concentrations inhibited the synthesis of DNA, RNA, protein and carbohydrate contents. The degree of inhibition increased with increasing toxicant concentrations. Protein content was the most sensitive macromolecule affected by lindane.

5.
Parasitology ; 74(3): 299-312, 1977 Jun.
Article in English | MEDLINE | ID: mdl-327402

ABSTRACT

An initial observation concerning the failure of [3H]thymidine at high specific activity to be incorporated into the DNA of Crithidia fasciculata for more than a brief initial period has been correlated with the presence at high specific activity in the organism of a thymidine phosphorylase activity with an equilibrium in the direction of catabolism. This enzyme degrades thymidine to thymine which is not utilized by the organism. The enzyme has also been shown to be present in a number of other trypanosomatids, including the culture forms of Trypanosoma cruzi, where the specific activity was nearly as high as that in C. fasciculata. Evidence is presented that in C. fasciculata, the culture forms of T. cruzi and possibly other species of trypanosomatid, the thymidine phosphorylae, together with a thymidylate phosphatase, forms a catabolic pathway which degrades thymine nucleotides to thymine, which is then excreted. About 60% of the thymine nucleotides made by organisms appear to be metabolized through the pathway, suggesting that their synthesis is not subject to completely effective regulatory control.


Subject(s)
Eukaryota/enzymology , Thymidine Monophosphate/metabolism , Thymine Nucleotides/metabolism , Animals , Nucleotidases/metabolism , Thymidine/metabolism , Thymidine Phosphorylase/metabolism , Thymine/metabolism , Trypanosoma brucei brucei/enzymology , Trypanosoma brucei brucei/metabolism , Trypanosoma cruzi/enzymology , Trypanosoma cruzi/metabolism , Uracil/metabolism
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