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The glutathione transferase activity and tissue distribution of a cloned Mr28K protective antigen of Schistosoma mansoni.
Author(s) -
Taylor J. B.,
Vidal A.,
Torpier G.,
Meyer D. J.,
Roitsch C.,
Balloul J. M.,
Southan C.,
Sondermeyer P.,
Pemble S.,
Lecocq J. P.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb02834.x
Subject(s) - biology , schistosoma mansoni , glutathione s transferase , antigen , glutathione transferase , glutathione , schistosoma , tissue distribution , microbiology and biotechnology , virology , schistosomiasis , immunology , helminths , enzyme , biochemistry , physiology
A protective Mr28K antigen of Schistosoma mansoni, expressed from its cDNA, has been purified in a single step and shown to possess glutathione (GSH) transferase activity as predicted from sequence homologies with two mammalian GSH transferase multigene families. It is notable for its high 1‐chloro‐2,4‐dinitrobenzene GSH transferase and linoleic acid hydroperoxide GSH peroxidase activities. The major GSH transferase of S. mansoni has been purified and its subunit is identical to this Mr28K antigen by criteria of Mr, immunochemistry, substrate specificity and peptide sequence analysis. In the parasite, the antigen is present in the tegument, protonephridial cells and subtegumental parenchymal cells. No significant immunological cross‐reactivity between the S.mansoni and mammalian (human and rat) GSH transferases was observed.