Literature DB >> 11853961

Glutathione transferase isoenzymes from frog (Xenopus laevis) liver and embryo.

Stefania Angelucci1, Paolo Sacchetta, Antonella De Luca, Pasquale Moio, Fernanda Amicarelli, Carmine Di Ilio.   

Abstract

The expression of glutathione transferase isoenzymes has been investigated in embryo and adult liver of the frog Xenopus laevis. By analysing the GST isoenzymes recovered from GSH-affinity chromatography in terms of electrophoretic mobility, HPLC elution profile, immunological reactivity, N-terminal amino acid sequence and mass spectrometry molecular mass no significant difference in the GST subunit composition between embryos and liver was found. In both tissues the same three subunits, showing similarity to mu, alpha and sigma class GSTs, are present. These results, together with those previously reported for toad (Bufo bufo), strongly support the notion that the transition from an aquatic environment to a terrestrial atmosphere containing high oxygen concentration has accompanied specific GST gene expression.

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Year:  2002        PMID: 11853961     DOI: 10.1016/s0304-4165(01)00238-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Mu-class glutathione transferase from Xenopus laevis: molecular cloning, expression and site-directed mutagenesis.

Authors:  Antonella De Luca; Bartolo Favaloro; Stefania Angelucci; Paolo Sacchetta; Carmine Di Ilio
Journal:  Biochem J       Date:  2002-08-01       Impact factor: 3.857

2.  A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site.

Authors:  Antonella De Luca; Bartolo Favaloro; Erminia Carletti; Paolo Sacchetta; Carmine Di Ilio
Journal:  Biochem J       Date:  2003-07-15       Impact factor: 3.857

  2 in total

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