Literature DB >> 6411491

The amount and nature of glutathione transferases in rat liver microsomes determined by immunochemical methods.

R Morgenstern, C Guthenberg, B Mannervik, J W DePierre.   

Abstract

The amount and nature of glutathione transferases in rat liver microsomes were determined using immunological techniques. It was shown that cytosolic glutathione transferase subunits A plus C, and B plus L were present at levels of 2.4 +/- 0.6 and 1.5 +/- 0.1 microgram/mg microsomal protein, respectively. These levels are 10-times higher than those for non-specific binding of cytosolic components judging from the distribution of lactate dehydrogenase, a cytosolic marker. The possibility that a portion of these glutathione transferases is functionally localized on the endoplasmic reticulum is discussed. A previously described microsomal glutathione transferase which is distinct from the cytosolic enzymes is present in an amount of 31 +/- 6 micrograms/mg microsomal protein.

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Year:  1983        PMID: 6411491     DOI: 10.1016/0014-5793(83)80979-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Activation of rat liver microsomal glutathione transferase by limited proteolysis.

Authors:  R Morgenstern; G Lundquist; H Jörnvall; J W DePierre
Journal:  Biochem J       Date:  1989-06-01       Impact factor: 3.857

2.  Leukotriene C synthase in mouse mastocytoma cells. An enzyme distinct from cytosolic and microsomal glutathione transferases.

Authors:  M Söderström; S Hammarström; B Mannervik
Journal:  Biochem J       Date:  1988-03-15       Impact factor: 3.857

3.  Inhibition of microsomal lipid peroxidation by glutathione and glutathione transferases B and AA. Role of endogenous phospholipase A2.

Authors:  K H Tan; D J Meyer; J Belin; B Ketterer
Journal:  Biochem J       Date:  1984-05-15       Impact factor: 3.857

  3 in total

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