Purification and characterization of glutathione S-transferases from rat pancreas

Sharad S. Singhal, Sanjiv Gupta, Manju Saxena, Rajendra Sharma, Hassan Ahmad, G. A.S. Ansari, Yogesh C. Awasthi

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Glutathione S-transferases (GSTs) of rat pancreas have been characterized and their interrelationship with fatty acid ethyl ester synthase (FAEES) has been studied. Seven GST isozymes with pI values of 9.2, 8.15, 7.8, 7.0, 6.3, 5.9 and 5.4 have been isolated and designated as rat pancreas GST suffixed by their pI values. Structural, immunological and kinetic properties of these isozymes indicated that GST 9.2 belonged to the α class, GST 7.8, 7.0, 6.3 and 5.9 belonged to the μ class, whereas GST 8.15 and 5.4 belong to π class. The N-terminal sequences and pI values of the μ class isozymes suggested that rat GST subunits 3, 4 and 6 may be expressed in pancreas. N-Terminal sequences of both the π class isozymes, GST 8.15 and 5.4, were similar to that of GST-P, but there were significant differences in the substrate specificities of these two enzymes. Results of peptide finger print studies also indicated minor structural differences between these two isozymes. None of the GST isozymes of rat pancreas expressed FAEES activity. Rat pancreas had a significant amount of FAEES activity, but it segregated independently during the purification of GST indicating that these two activities are expressed by different proteins and are not related as suggested previously.

Original languageEnglish (US)
Pages (from-to)285-292
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number3
StatePublished - Sep 20 1991
Externally publishedYes


  • Fatty acid ethyl ester synthase
  • Glutathione
  • Glutathione S-transferases
  • Pancreas

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology
  • Biophysics
  • Biochemistry


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