Glutathione S-transferase composition of rat erythrocytes.
With 1-chloro-2,4-dinitrobenzene as the electrophilic substrate, the specific activity of glutathione S-transferase in rat haemolysates was found to range from 0.002 to 0.013 mumol/min/mg haemoglobin at 30 degrees C. To establish the glutathione S-transferase composition, chromatofocusing was used which indicated the presence of a single soluble isoenzyme with an apparent pI of 6.1. A molecular weight of 48,000 was determined for the enzyme by gel filtration. The transferase enzyme in intact erythrocytes is shown to catalyze the formation of S-(2,4-dinitrophenyl)-glutathione from 1-chloro-2,4-dinitrobenzene and endogenous glutathione. Efflux of this conjugate from erythrocytes proceeded at a rate of 13 nmol/min/ml at 37 degrees C.
Department of Biochemistry, Rand Afrikaans University, Johannesburg, South Africa.
H W
HW
Dirr
J C
JC
Schabort
D000818:Animals; D004912:Erythrocytes / Q000201:enzymology*; D005982:Glutathione Transferase / Q000097:blood* / Q000302:isolation & purification; D051381:Rats; D011919:Rats, Inbred Strains
D005982:Glutathione Transferase