Glutathione transferase isoenzymes from human testis.
By using affinity chromatography and isoelectric focusing techniques, several forms of glutathione transferase (GSTs) were resolved from human testis obtained from patients operated on for malignant diseases. Large interindividual variations in the expression of different isoenzymes resulted in the samples investigated. Five out of six samples analysed expressed GST-4.4 that resulted in being structurally and immunologically identical to GST-pi (class Pi). All the cationic GSTs of human testis, except for GST-8.36, GST-9.1 and GST-10.1, are homodimers of 24,500 Mr subunit and cross reacted with antisera raised against class Alpha GST. Some of the forms isolated (GST-3.8, GST-8.36, GST-9.1 and GST-10.1) can not apparently be related to any of GSTs so far characterized in other human tissues. Upon SDS/polyacrylamide gel electrophoresis, GST-8.36 and GST-9.1 appeared to be heterodimers of 24,500 and 26,500 Mr subunits and were found only in the testis seminoma suggesting that they might be tumour specific isoenzymes. GST-3.8 appeared to be formed by heterodimers of 23,000 and 26,500 Mr subunits whereas, GST-10.1 was found to be dimers of 22,000 and 24,500 Mr subunits. In addition, the results of immunohistochemical studies with antisera raised against both class Pi and Alpha GSTs are reported.
Aceto
A
A
Instituto di Scienze Biochimiche, Facolta di Medicina, Universita G. D'Annunzio, Chieti, Italy.
Di Ilio
C
C
Angelucci
S
S
Felaco
M
M
Federici
G
G
D000368:Aged; D002846:Chromatography, Affinity; D005982:Glutathione Transferase / Q000302:isolation & purification*; D006801:Humans; D007124:Immunoenzyme Techniques; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification*; D008297:Male; D013737:Testis / Q000201:enzymology* / Q000648:ultrastructure
D007527:Isoenzymes; D005982:Glutathione Transferase