Literature DB >> 22573

A simple method to determine gammaglutamyl-cyclotransferase activity in erythrocytes.

P G Board, J E Smith, K Moore.   

Abstract

A new method for the determination of erythrocyte gammaGCT is described. The method follows the release of alanine from gammaglutamyl alanine by a series of linked reactions that result in the oxidation of NADH to NAD. The pH optimum for human erythrocyte gammaGCT was found to be 9.0, and the Km for gammaglutamyl alanine was found to be 2.3 X 10(-3) M. Human erythrocytes had the highest activity of all the species studied (human, rabbit, dog, sheep, cattle, chicken).

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Year:  1978        PMID： 22573

Source DB:  PubMed          Journal:  J Lab Clin Med        ISSN： 0022-2143


  2 in total

1.  Purification and properties of gamma-glutamylcyclotransferase from human erythrocytes.

Authors:  P G Board; K A Moore; J E Smith
Journal:  Biochem J       Date:  1978-08-01       Impact factor: 3.857

2.  Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism.

Authors:  Aaron J Oakley; Marjorie Coggan; Philip G Board
Journal:  J Biol Chem       Date:  2010-01-28       Impact factor: 5.157
  2 in total

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