Literature DB >> 6108786

Erythrocyte gamma-glutamylcysteine synthetase from normal and low-glutathione sheep.

P G Board, J E Smith, K Moore, D Ou.   

Abstract

gamma-Glutamylcysteine synthetase (L-glutamate:L-cysteine gamma-ligase (ADP-forming), EC 6.3.2.2) was purified from the erythrocytes of normal and low-glutathione sheep. The molecular weight (78 000), pH optimum (pH 7), substrate specificity, inhibition constant for glutathione (0.44-0.50 mM), electrophoretic mobility, and heat stability were similar for the purified enzyme from both sources. Using immunological techniques, the specific activity of gamma-glutamylcysteine synthetase from low-glutathione sheep was lower than that from normal sheep.

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Year:  1980        PMID: 6108786     DOI: 10.1016/0005-2744(80)90109-6

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


  3 in total

1.  Kinetic characteristics of native gamma-glutamylcysteine ligase in the aging housefly, Musca domestica L.

Authors:  Dikran Toroser; Rajindar S Sohal
Journal:  Biochem Biophys Res Commun       Date:  2005-01-21       Impact factor: 3.575

2.  Identification of an essential cysteine residue in human glutathione synthase.

Authors:  R R Gali; P G Board
Journal:  Biochem J       Date:  1997-01-01       Impact factor: 3.857

3.  Abnormal gamma-glutamylcysteine synthetase activities in sheep red blood cells.

Authors:  E M Tucker; L Kilgour; C Crowley; J D Young
Journal:  Biochem Genet       Date:  1983-10       Impact factor: 1.890

  3 in total

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