Specific recognition of human π glutathione transferase by an antipeptide antibody

• Published in: Biochimica et biophysica acta Vol. 1074; no. 1; pp. 214 - 216
• Main Authors: Evangelista, Michele, Chersi, Alberto, Citro, Gennaro
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 24.05.1991; Elsevier
• Subjects: Amino Acid Sequence; Animals; Antibodies - immunology; Antipeptide antibody; Biological and medical sciences; Glutathione transferase; Glutathione Transferase - analysis; Glutathione Transferase - immunology; Host-tumor relations. Immunology. Biological markers; Humans; Medical sciences; Molecular Sequence Data; Peptide Fragments - immunology; Rabbits; Tumor marker; Tumors; Tumor marker; Glutathione transferase; Bzl; KLH; Boc; DIPC; TFMSA; Z; Antipeptide antibody; DMF; DCM; Sequence specificity; Immunization; Peptides; Rat; Antibody; Enzyme; Rodentia; Rabbit; Tumoral marker; Lagomorpha; Vertebrata; Mammalia; Binding capacity; Enzymatic activity; Molecular complex; ELISA assay
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(91)90064-N

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-π), 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.