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Pyridoxine Kinase in Plasmodium lophurae and Duckling Erythrocytes *
Author(s) -
PLATZER EDWARD G.,
KASSIS JUDITH A.
Publication year - 1978
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.1550-7408.1978.tb04186.x
Subject(s) - pyridoxine , enzyme , plasmodium (life cycle) , biology , biochemistry , kinase , parasite hosting , microbiology and biotechnology , chemistry , world wide web , computer science
SYNOPSIS. Pyridoxine kinase enzyme activity was greatly increased in duckling erythrocytes infected with Plasmodium lophurae. Pyridoxine kinase activity in parasites freed from erythrocytes was much greater than that of uninfected erythrocytes. The apparent K m for pyridoxine of the parasite enzyme was 6.6 × 10 ‐5 M whereas the host red cell enzyme K m was 1.9 × 10 ‐6 M. Deoxypyridoxine inhibited host and parasite pyridoxine kinase activity with an apparent K i of 1.5 × 10 ‐6 and 8.6 × 10 ‐6 M, respectively. These results suggest that the vitamin B 6 metabolism of the malaria parasites is distinct and separate from that of the host erythrocytes.