Specific recognition of human pi glutathione transferase by an antipeptide antibody.

Abstract

Antibodies were raised in a rabbit by using a 12-residue synthetic peptide, corresponding to fragment 2-13 of rat placental glutathione S-transferase, as the immunogen. The antiserum appeared to react with the fragment as well as with the corresponding human enzyme (GST-pi), which shares with the rat transferase a 92% sequence homology at the N terminus. In addition, the binding of the antibody to the protein was completely inhibited by small amounts of peptide. The enzymatic activity of glutathione transferase was not affected by the antibody. This might indicate that the N-terminal fragment is not involved in the catalytic activity of the enzyme. This antibody of predetermined specificity might thus find a useful application for the detection and approximate quantitation of this marker in human preneoplastic lesions.

Cite this paper

@article{Evangelista1991SpecificRO, title={Specific recognition of human pi glutathione transferase by an antipeptide antibody.}, author={Marco Evangelista and Alberto Chersi and Gennaro Citro}, journal={Biochimica et biophysica acta}, year={1991}, volume={1074 1}, pages={214-6} }