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

A.E.A Thumser; P.A Adams

doi:10.1016/0162-0134(94)80001-4

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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

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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

A.E.A Thumser and P.A Adams

Journal of inorganic biochemistry, Vol.53(3), pp.157-168

1994

DOI: https://doi.org/10.1016/0162-0134(94)80001-4

PMID: 8133252

Abstract

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 K i, 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-π.

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Title: 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
Creators: A.E.A Thumser - Department of Medical Biochemistry University of Cape Town Medical School, Observatory, Cape Town, South Africa
P.A Adams - MRC Biomembrane Research Unit, Department of Chemical Pathology, University of Cape Town Medical School, Observatory, Cape Town, South Africa
Publication Details: Journal of inorganic biochemistry, Vol.53(3), pp.157-168
Publisher: Elsevier Inc
Date published: 1994
Identifiers: 99586584702346
Language: English
Resource Type: Journal article

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

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