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Characteristics of Cytidine Aminohydrolase Activity in Trypanosoma cruzi and Crithidia fasciculata 1
Author(s) -
KIDDER GEORGE W.
Publication year - 1984
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1984.tb02965.x
Subject(s) - crithidia fasciculata , cytidine , trypanosoma cruzi , cytidine deaminase , biochemistry , enzyme , biology , uridine , chemistry , microbiology and biotechnology , rna , parasite hosting , world wide web , computer science , gene
Cytidine deaminase (cytidine aminohydrolase, 3.5.4.5) is present in Crithidia fasciculata (a mosquito parasite) and in Trypanosoma cruzi (a human pathogen). The enzyme from C. fasciculata deaminated both cytidine and deoxycytidine, the affinity for the former being much lower than the latter. Affinities for both substrates are equal for the T. cruzi enzyme. The production of the enzyme in C. fasciculata was significantly stimulated by the addition of a number of pyrimidine nucleosides (cytidine, uridine, 5‐bromouridine, thymidine, orotidine) to the culture media. Only cytidine stimulated enzyme production in T. cruzi . The enzyme from both organisms was unstable in air, even in the frozen state. Stabilization was achieved under anaerobic conditions.