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Pantothenic Acid Metabolism During Avian Malaria Infection: Pantothenate Kinase Activity in Duck Erythrocytes and in Plasmodium lophurae *
Author(s) -
BENNETT THOMAS PETER,
TRAGER WILLIAM
Publication year - 1967
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.1550-7408.1967.tb01985.x
Subject(s) - pantothenic acid , biology , plasmodium (life cycle) , avian malaria , biochemistry , metabolism , enzyme , coenzyme a , cofactor , virology , malaria , parasite hosting , immunology , plasmodium falciparum , gametocyte , vitamin , world wide web , computer science , reductase
SYNOPSIS. The initial enzymatic reaction in the pathway of coenzyme A genesis from pantothenic acid, i.e., the conversion of pantothenic acid to phosphopantothenic acid catalyzed by pantothenic acid kinase, was found in extracts of avian erythrocytes but not in extracts of Plasmodium lophurae or intact parasites. The activity of the kinase was significantly higher in extracts prepared from normal duck erythrocytes than those infected with P. lophurae. The apparent absence of pantothenic acid kinase in P. lophurae is corroborative support for nutritional studies(7,9) which suggest that the avian malarial parasite is dependent for its supply of coenzyme A on the host cell.