Anionic glutathione S-transferases in shrimp eyes.
1. Two anionic isoenzymes of glutathione transferases (EC 2.5.1.18), QI and QII, have been purified from the eyes of the shrimp Penaeus japonicus by using a combination of S-hexylglutathione affinity column chromatography and Mono-Q fast protein liquid chromatography (f.p.l.c.). 2. Both QI and II glutathione S-transferases are homodimers. They show similarity in substrate specificities and pH optima, but not in isoelectric points. 3. QI is distinct from QII by anion-exchange f.p.l.c., reverse-phase h.p.l.c. chromatography and amino acid sequencing analysis. QI has N-terminal amino acid sequences homologous to mu glutathione S-transferase, whereas QII is homologous to theta glutathione S-transferases.
Lin
K S
KS
Division of Biochemistry and Molecular Science, Academia Sinica, Nankang, Taipei, Taiwan, Republic of China.
Chuang
N N
NN
D000595:Amino Acid Sequence; D000818:Animals; D000838:Anions; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D033364:Decapoda / Q000201:enzymology*; D005123:Eye / Q000201:enzymology; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification*; D007700:Kinetics; D008969:Molecular Sequence Data
D000838:Anions; D007527:Isoenzymes; D005982:Glutathione Transferase