Aldolase in the culture form of Trypanosoma cruzi
| Autor: | Harry D. Baernstein, C.W. Rees |
|---|---|
| Rok vydání: | 1952 |
| Předmět: |
chemistry.chemical_classification
Immunology Aldolase A General Medicine Isomerase Biology biology.organism_classification Phosphate Pyrophosphate Michaelis–Menten kinetics chemistry.chemical_compound Infectious Diseases Enzyme chemistry Biochemistry Iodoacetamide biology.protein Parasitology Trypanosoma cruzi |
| Zdroj: | Experimental Parasitology. 1:215-228 |
| ISSN: | 0014-4894 |
| DOI: | 10.1016/0014-4894(52)90012-x |
| Popis: | 1. 1. Aldolase has been demonstrated in homogenates of the culture form of T. cruzi by three methods for estimating the triose phosphate produced. 2. 2. The limits within which linearity of color production with respect to time and to concentration of enzyme exist have been determined. 3. 3. The Michaelis constant was found to be 1.2 × 10−3M HDP. 4. 4. Optimum pH was 7.3 in collidine buffer. 5. 5. Optimum temperature was about 45 °C. 6. 6. Aldolase in homogenates of T. cruzi was unstable when stored for several days at 5 °C. Freezing or dialysis hastened inactivation. Such inactive samples could not be reactivated by cysteine and/or ferrous ions. 7. 7. Copper sulfate inactivated the enzyme completely; pyrophosphate, 8-hydroxyquinoline, iodoacetamide somewhat less. 8. 8. Dipyridyl had no effect on the activity, and no evidence that this is a metal-activated aldolase was obtained. 9. 9. Aldolase activity per gram wet weight of organisms was equivalent to 0.03 Meyerhof units. This indicates that T. cruzi (culture form) has a very low aldolase activity, and in connection with other calculations, indicates that the organism probably makes considerable use of non-glucose substrates. 10. 10. Indirect evidence for the existence of isomerase is presented. |
| Databáze: | OpenAIRE |
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