Purification and characterization of glutathione S-transferases of human kidney

S. V. Singh, T. Leal, G. A.S. Ansari, Y. C. Awasthi

Research output: Contribution to journalArticle

67 Scopus citations

Abstract

Several forms of glutathione S-transferase (GST) are present in human kidney, and the overall isoenzyme pattern of kidney differs significantly from those of other human tissues. All the three major classes of GST isoenzymes (α, μ and π) are present in significant amounts in kidney, indicating that GST1, GST2 and GST3 gene loci are expressed in this tissue. More than one form of GST is present in each of these classes of enzyme, and individual variations are observed for these classes. The structural, immunological and functional properties of GST isoenzymes of three classes differ significantly from each other, whereas the isoenzymes belonging to the same class have similar properties. All the cationic GST isoenzymes of human kidney except for GST 9.1 are heterodimers of 26,500-M(r) and 24,500-M(r) subunits. GST 9.1 is a dimer of 24,500-M(r) subunits. All the cationic isoenzymes of kidney GST cross-react with antibodies raised against a mixture of GST α, β, γ, δ and ε isoenzymes of liver. GST 6.6 and GST 5.5 of kidney are dimers of 26,500-M(r) subunits and are immunologicaly similar to GST ψ of liver. Unlike other human tissues, kidney has at least two isoenzymes (pI 4.7 and 4.9) associated with the GST3 locus. Both these isoenzymes are dimers of 22,500-M(r) subunits and are immunologically similar to GST π of placenta. Some of the isoenzymes of kidney do not correspond to known GST isoenzymes from other human tissues and may be specific to this tissue.

Original languageEnglish (US)
Pages (from-to)179-186
Number of pages8
JournalBiochemical Journal
Volume246
Issue number1
DOIs
StatePublished - Jan 1 1987

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this