Haem peptide/protein interaction. Part 6: The kinetic mechanisms of the interactions with, and inhibition of enzymic activity of the human erythrocyte glutathione S-transferase isoenzyme rho (p), by haem octa-, nona-, and undecapeptides MP-8/-9/-11.
The binding of the cytochrome-c derived haem peptides microperoxidase-8, -9, and -11 (MP-8, -9, and -11) to the human erythrocyte glutathione S-transferase rho (GST-p) enzyme is demonstrated. Inhibition by the haem peptides of the enzymic conjugation of glutathione (GSH) with the electrophilic cosubstrate 1-chloro-2, 4-dinitrobenzene (CDNB) is mixed-type with respect to CDNB, and Ki, the inhibition constant, increases with increasing length of the peptide chain. The results obtained here for the GST-p are compared to those published recently for the previously-supposed identical isoenzyme human placental GST-pi.
Thumser
A E
AE
Department of Medical Biochemistry, University of Cape Town Medical School, Observatory, South Africa.
Adams
P A
PA
D004912:Erythrocytes / Q000201:enzymology; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000097:blood*; D006420:Hemeproteins / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000097:blood*; D007700:Kinetics; D008024:Ligands; D009842:Oligopeptides / Q000378:metabolism / Q000494:pharmacology; D010544:Peroxidases / Q000378:metabolism / Q000494:pharmacology
D006420:Hemeproteins; D007527:Isoenzymes; D008024:Ligands; D009842:Oligopeptides; D010544:Peroxidases; C021799:microperoxidase; D005982:Glutathione Transferase