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A purine nucleoside hydrolase from Trypanosoma gambiense, purification and properties.
- Source :
-
Tropenmedizin und Parasitologie [Tropenmed Parasitol] 1975 Mar; Vol. 26 (1), pp. 19-26. - Publication Year :
- 1975
-
Abstract
- A purine nucleoside hydrolase from Trypanosoma gambiense was purified 160-fold. Preferred substrates of the reaction were adenosine, inosine and guanosine with a maximum of activity at pH 5.4. Competitive inhibitors of the adenosine hydrolysis were dimethylallyl adenosine, 6-methylmercaptopurine riboside, tubercidin, formycin B, 6-mercaptopurine riboside and deoxyadenosine. A metabolic scheme of adenosine nomophosphate salvage synthesis is discussed.
- Subjects :
- Adenine Phosphoribosyltransferase isolation & purification
Adenosine metabolism
Adenosine Kinase isolation & purification
Adenosine Monophosphate biosynthesis
Animals
Cell-Free System
Chromatography
Chromatography, DEAE-Cellulose
Guanosine
Hydrogen-Ion Concentration
Hypoxanthine Phosphoribosyltransferase isolation & purification
Inosine
Isoelectric Focusing
Ligases isolation & purification
N-Glycosyl Hydrolases antagonists & inhibitors
Oxidative Phosphorylation
Purine Nucleosides
Purine Nucleotides biosynthesis
Trypanosoma brucei gambiense metabolism
N-Glycosyl Hydrolases isolation & purification
Trypanosoma brucei gambiense enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0303-4208
- Volume :
- 26
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Tropenmedizin und Parasitologie
- Publication Type :
- Academic Journal
- Accession number :
- 238316