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The Sites of Action of Allopurinol in Crithidia fasciculata *
Author(s) -
DEWEY VIRGINIA C.,
KIDDER G. W.
Publication year - 1973
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.1550-7408.1973.tb03597.x
Subject(s) - crithidia fasciculata , allopurinol , hypoxanthine , biochemistry , purine , xanthine , chemistry , crithidia , enzyme , uric acid , purine metabolism , phosphate , stereochemistry , biology , medicine , genetics , pathology , protozoa
SYNOPSIS Reversal of the growth inhibition of Crithidia fasciculata by allopurinol requires both a purine and a pyrimidine. Hypoxanthine is the most effective purine in the reversal. Cell‐free extracts were prepared which were capable of the decarboxylation of orotidine 5′‐phosphate. Other enzyme preparations carried out the phosphoribosylation of allopurinol. By the use of [4‐ 14 C] orotidine 5′‐phosphate (enzymatically prepared), it was shown that allopurinol ribotide (enzymatically prepared), but not the free base, inhibits orotidine 5′‐phosphate decarboxylase.