Literature DB >> 12514067

Glutathione S-transferase isoenzymes from Streptomyces griseus.

Kajari Dhar1, Alok Dhar, John P N Rosazza.   

Abstract

An inducible, cytosolic glutathione S-transferase (GST) was purified from Streptomyces griseus. GST isoenzymes with pI values of 6.8 and 7.9 used standard GST substrates including 1-chloro-2,4-dinitrobenzene. GST had subunit and native M(r)s of 24 and 48, respectively, and the N-terminal sequence SMILXYWDIIRGLPAH.

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Year:  2003        PMID: 12514067      PMCID: PMC152383          DOI: 10.1128/AEM.69.1.707-710.2003

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  27 in total

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Authors:  K Dhar; J P Rosazza
Journal:  Appl Environ Microbiol       Date:  2000-11       Impact factor: 4.792

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Journal:  Arch Biochem Biophys       Date:  1988-03       Impact factor: 4.013

10.  Purification and characterization of three forms of glutathione transferase from Proteus mirabilis.

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Journal:  Biochem J       Date:  1988-11-01       Impact factor: 3.857

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  3 in total

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Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-01-18

2.  Unusual production of glutathione in Actinobacteria.

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3.  Characterization of the Glutathione S-Transferases Involved in Styrene Degradation in Gordonia rubripertincta CWB2.

Authors:  Anna C Lienkamp; Jan Burnik; Thomas Heine; Eckhard Hofmann; Dirk Tischler
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