Literature DB >> 6612222

Isoelectric focusing of glutathione S-transferases: comparison of the acidic transferases from human liver, kidney, lung, spleen and placenta.

K Koskelo.   

Abstract

The glutathione S-transferase composition of human liver, kidney, lung, spleen and placenta was studied by density gradient isoelectric focusing. On the basis of the enzyme distribution it was possible to divide the supernatants into two groups: one having a predominance of basic activity, the other acidic. Each supernatant consisted of more than one transferase. Human liver and kidney, two major detoxifying organs in the body, bore a clear predominance of basic enzymes and they had the highest transferase activities. The activity of the other organs consisted of almost only a single acidic transferase. Properties of the major acidic transferases from the organs were compared. Prior to the studies the enzymes underwent partial two-step purification. According to the comparison it seems evident that the major acidic transferases from human kidney, lung, spleen and placenta are either closely related or identical.

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Year:  1983        PMID: 6612222     DOI: 10.1080/00365518309168235

Source DB:  PubMed          Journal:  Scand J Clin Lab Invest        ISSN: 0036-5513            Impact factor:   1.713


  7 in total

1.  Two distinct forms of glutathione transferase from human foetal liver. Purification and comparison with isoenzymes isolated from adult liver and placenta.

Authors:  C Guthenberg; M Warholm; A Rane; B Mannervik
Journal:  Biochem J       Date:  1986-05-01       Impact factor: 3.857

2.  H.p.l.c. separation and study of the charge isomers of human placental glutathione transferase.

Authors:  L L Radulovic; A P Kulkarni
Journal:  Biochem J       Date:  1986-10-01       Impact factor: 3.857

3.  Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver.

Authors:  P K Stockman; L I McLellan; J D Hayes
Journal:  Biochem J       Date:  1987-05-15       Impact factor: 3.857

4.  Use of immuno-blot techniques to discriminate between the glutathione S-transferase Yf, Yk, Ya, Yn/Yb and Yc subunits and to study their distribution in extrahepatic tissues. Evidence for three immunochemically distinct groups of transferase in the rat.

Authors:  J D Hayes; T J Mantle
Journal:  Biochem J       Date:  1986-02-01       Impact factor: 3.857

5.  Raised plasma glutathione S-transferase values in hyperthyroidism and in hypothyroid patients receiving thyroxine replacement: evidence for hepatic damage.

Authors:  G J Beckett; H A Kellett; S M Gow; A J Hussey; J D Hayes; A D Toft
Journal:  Br Med J (Clin Res Ed)       Date:  1985-08-17

6.  Species differences in the biotransformation of ethyl chloride. II. GSH-dependent metabolism.

Authors:  N Fedtke; H Certa; R Ebert; H J Wiegand
Journal:  Arch Toxicol       Date:  1994       Impact factor: 5.153

7.  Plasma glutathione S-transferase measurements after paracetamol overdose: evidence for early hepatocellular damage.

Authors:  G J Beckett; B J Chapman; E H Dyson; J D Hayes
Journal:  Gut       Date:  1985-01       Impact factor: 23.059

  7 in total

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