Literature DB >> 18597274

Deactivation of catalase by hydrogen peroxide.

P T Vasudevan1, R H Weiland.   

Abstract

When a mechanism is used to determine possible deactivation kinetics, a certain consistency with the kinetics of the main reaction is found. This result is examined in the light of experimental evidence obtained with bovine liver and Aspergillus catalases.

Entities:  

Year:  1990        PMID： 18597274     DOI： 10.1002/bit.260360805

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN： 0006-3592            Impact factor:   4.530


  4 in total

1.  Protecting peroxidase activity of multilayer enzyme-polyion films using outer catalase layers.

Authors:  Haiyun Lu; James F Rusling; Naifei Hu
Journal:  J Phys Chem B       Date:  2007-12-05       Impact factor: 2.991

2.  Soluble and immobilized catalase. Effect of pressure and inhibition on kinetics and deactivation.

Authors:  P T Vasudevan; D S Thakur
Journal:  Appl Biochem Biotechnol       Date:  1994-12       Impact factor: 2.926

3.  A chemiluminescence-based catalase assay using H2O2-sensitive CdTe quantum dots.

Authors:  Fahimeh Ghavamipour; Reza H Sajedi; Khosro Khajeh
Journal:  Mikrochim Acta       Date:  2018-07-16       Impact factor: 5.833

4.  A Kinetic Platform to Determine the Fate of Hydrogen Peroxide in Escherichia coli.

Authors:  Kristin J Adolfsen; Mark P Brynildsen
Journal:  PLoS Comput Biol       Date:  2015-11-06       Impact factor: 4.475
  4 in total

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