Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.5.1.18 (glutathione S-transferase)
 22,582 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cord factor (a mycobacterial toxin) treatment of mice for 72 hr resulted in decreased activities of hepatic drug metabolizing enzymes. The toxin treated animals exhibited reduced levels of liver cytochrome P-450 and cytochrome b5, accompanied by significant lowering of NADPH-cytochrome c reductase and NADH-cytochrome b5 reductase activities. The hepatic activities of aminopyrine N-demethylase and aniline hydroxylase were diminished, while liver cytosolic glutathione S-transferase activity was inhibited in mice receiving the toxin. Earlier studies from this laboratory (J. K. Batra, Ph.D. Thesis, Delhi University, India, 1982) on the effects of experimental tuberculosis on hepatic drug metabolism revealed changes similar to the presently reported influence of cord factor on mouse liver microsomal monooxygenases. Thus, the action of cord factor (on hepatic drug metabolism) largely mimics the effects of tuberculosis infection.
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PMID:Effect of cord factor, a toxic glycolipid from Mycobacterium tuberculosis, on mouse liver drug metabolizing enzymes. 310 76

We report the establishment of a hybridoma cell line secreting the monoclonal antibody (mAb) HAV, which recognizes the coat (AV1) protein of tomato leaf curl New Delhi virus (ToLCNDV), a begomovirus. The cell line was obtained following immunization of mice with purified recombinant AV1 fused to glutathione S-transferase (GST). A single-chain variable fragment (scFv-SAV) was assembled from hybridoma cDNA, but sequence analysis revealed a single nucleotide deletion causing a frame shift that resulted in a 21-residue N-terminal truncation. The missing nucleotide was restored by in vitro site-directed mutagenesis to create scFv-RWAV. The binding properties of mAb HAV and the corresponding scFvs were characterized by western blot, ELISA and surface plasmon resonance spectroscopy. MAb HAV bound to AV1 with nanomolar affinity but reacted neither with the N-terminal region of the protein nor with the GST fusion partner. This suggested that the antibody recognized a linear epitope in a region of the coat protein that is conserved among begomoviruses. Both scFvs retained the antigen specificity of mAb HAV, although the dissociation rate constant of scFv-RWAV was tenfold greater than that of scFv-SAV, showing the importance of restoring the 21 N-terminal amino acids.
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PMID:Generation and characterization of a scFv against recombinant coat protein of the geminivirus tomato leaf curl New Delhi virus. 2010 47