The characterization of glutathione S-transferases from rat olfactory epithelium.

The glutathione S-transferases (GSTs) of rat olfactory epithelium have been characterized with regard to substrate specificity and subunit composition and compared to those of the liver. The presence of cytosolic GST activity in rat olfactory epithelium was confirmed and, using 1-chloro-2,4-dinitrobenzene as substrate, was found to be approximately one-third that of the liver. Olfactory microsomal GST activity was greater than that of liver microsomes and could be activated by treatment with the sulphydryl agent N-ethylmaleimide. The subunit and isoenzyme profile of GSTs in the olfactory epithelium was investigated using a number of techniques. (1) Olfactory GSTs were characterized using a range of relatively subunit-specific substrates. Activities ranged from 40-90% of those found in liver. Most noticeable was the extremely low olfactory activity with the substrate specific for subunit 1. (2) Immunoblotting with antibodies against specific rat hepatic GSTs confirmed the presence of a number of subunits and the absence of subunit 1. (3) F.p.l.c. chromatofocusing and reverse-phase h.p.l.c. indicated that the cytosolic GST profile of olfactory epithelium is unique and is made up of subunits 2, 3, 4, 7, 8 and 11 with subunits 3 and 4 predominating. There is an absence of isoenzymes containing subunit 1.