Glutathione transferase isoenzymes from frog (Xenopus laevis) liver and embryo.
The expression of glutathione transferase isoenzymes has been investigated in embryo and adult liver of the frog Xenopus laevis. By analysing the GST isoenzymes recovered from GSH-affinity chromatography in terms of electrophoretic mobility, HPLC elution profile, immunological reactivity, N-terminal amino acid sequence and mass spectrometry molecular mass no significant difference in the GST subunit composition between embryos and liver was found. In both tissues the same three subunits, showing similarity to mu, alpha and sigma class GSTs, are present. These results, together with those previously reported for toad (Bufo bufo), strongly support the notion that the transition from an aquatic environment to a terrestrial atmosphere containing high oxygen concentration has accompanied specific GST gene expression.
Angelucci
Stefania
S
Dipartmento di Scienze Biomediche, Università G. D'Annuzuio, Chieti, Italy.
Sacchetta
Paolo
P
De Luca
Antonella
A
Moio
Pasquale
P
Amicarelli
Fernanda
F
Di Ilio
Carmine
C
D000595:Amino Acid Sequence; D000818:Animals; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004625:Embryo, Nonmammalian / Q000201:enzymology*; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification*; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D014982:Xenopus laevis / Q000196:embryology / Q000378:metabolism*
D007527:Isoenzymes; D005982:Glutathione Transferase