Human glutathione S-transferases. Characterization of the anionic forms from lung and placenta

D. D. Dao, C. A. Partridge, A. Kurosky, Y. C. Awasthi

    Research output: Contribution to journalArticle

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    Abstract

    Anionic glutathione S-transferases were purified from human lung and placenta. Chemical and immunochemical characterization, including polyacrylamide-gel electrophoresis, gave strong evidence that the anionic lung and placental enzymes are chemically similar, if not identical, proteins. The electrophoretic mobilities of both proteins were identical in conventional alkaline gels as well as in gels containing sodium dodecyl sulphate. Gel filtration of the intact active enzyme established an M(r) value of 45,000; however, with sodium dodecyl sulphate/polyacrylamide-gel electrophoresis under dissociating conditions a subunit M(r) of 22,500 was obtained. Amino acid sequence analysis of the N-terminal region of the placental enzyme revealed a single polypeptide sequence identical with that of lung. Results obtained from immunoelectrophoresis, immunotitration, double immunodiffusion and rocket immunoelectrophoresis also indicated the anionic lung and placental enzymes to be closely similar. The chemical similarity of these two proteins was further supported by protein compositional analysis and fragment analysis after chemical hydrolysis. Immunochemical comparison of the anionic lung and placental enzymes with human liver glutathione S-transferases revealed cross-reactivity with the anionic ω enzyme, but no cross-reactivity was detectable with the cationic enzymes. Comparison of the N-terminal region of the human anionic enzyme with reported sequences of rat liver glutathione S-transferases gave strong evidence of chemical similarity, indicating that these enzymes are evolutionarily related. However, computer analysis of the 30-residue N-terminal sequence did not show any significant chemical similarity to any other reported protein sequence, pointing to the fact that the glutathione S-transferases represent a unique class of proteins.

    Original languageEnglish (US)
    Pages (from-to)33-41
    Number of pages9
    JournalBiochemical Journal
    Volume221
    Issue number1
    StatePublished - 1984

    Fingerprint

    Glutathione Transferase
    Placenta
    Lung
    Enzymes
    Immunoelectrophoresis
    Proteins
    Gels
    Electrophoresis
    Sodium Dodecyl Sulfate
    Liver
    Polyacrylamide Gel Electrophoresis
    Electrophoretic mobility
    Immunodiffusion
    Protein Sequence Analysis
    Rockets
    Gel Chromatography
    Rats
    Hydrolysis
    Amino Acids
    Peptides

    ASJC Scopus subject areas

    • Biochemistry

    Cite this

    Dao, D. D., Partridge, C. A., Kurosky, A., & Awasthi, Y. C. (1984). Human glutathione S-transferases. Characterization of the anionic forms from lung and placenta. Biochemical Journal, 221(1), 33-41.

    Human glutathione S-transferases. Characterization of the anionic forms from lung and placenta. / Dao, D. D.; Partridge, C. A.; Kurosky, A.; Awasthi, Y. C.

    In: Biochemical Journal, Vol. 221, No. 1, 1984, p. 33-41.

    Research output: Contribution to journalArticle

    Dao, DD, Partridge, CA, Kurosky, A & Awasthi, YC 1984, 'Human glutathione S-transferases. Characterization of the anionic forms from lung and placenta', Biochemical Journal, vol. 221, no. 1, pp. 33-41.
    Dao, D. D. ; Partridge, C. A. ; Kurosky, A. ; Awasthi, Y. C. / Human glutathione S-transferases. Characterization of the anionic forms from lung and placenta. In: Biochemical Journal. 1984 ; Vol. 221, No. 1. pp. 33-41.
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