Literature DB >> 2489236

Experimental methods for kinetic study of suicide substrates.

F Garcia-Canovas1, J Tudela, R Varon, A M Vazquez.   

Abstract

The kinetic study of the enzymatic inactivation originated by suicide substrates can be carried out by means of two alternative approaches. One method considers the substrate concentration as practically constant during the assay time and provides explicit equations of product concentration vs. time. The other method involves the significant consumption of the substrate, yielding implicit equations of time vs. product concentration. The utility of both methods is discussed and adequate experimental conditions for their correct application are established.

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Year:  1989        PMID: 2489236     DOI: 10.3109/14756368909030367

Source DB:  PubMed          Journal:  J Enzyme Inhib        ISSN: 1026-5457


  4 in total

1.  Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.

Authors:  J C Espín; J Tudela
Journal:  Biochem J       Date:  1994-04-01       Impact factor: 3.857

2.  Kinetic study of the inactivation of ascorbate peroxidase by hydrogen peroxide.

Authors:  A N Hiner; J N Rodríguez-López; M B Arnao; E Lloyd Raven; F García-Cánovas; M Acosta
Journal:  Biochem J       Date:  2000-06-01       Impact factor: 3.857

3.  Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2.

Authors:  J Hernández-Ruiz; M B Arnao; A N Hiner; F García-Cánovas; M Acosta
Journal:  Biochem J       Date:  2001-02-15       Impact factor: 3.857

Review 4.  An updated review of tyrosinase inhibitors.

Authors:  Te-Sheng Chang
Journal:  Int J Mol Sci       Date:  2009-05-26       Impact factor: 6.208

  4 in total

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