Literature DB >> 428388

Validity of a 'steady-state' treatment of inactivation kinetics.

A Cornish-Bowden.   

Abstract

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Year:  1979        PMID： 428388     DOI： 10.1111/j.1432-1033.1979.tb12834.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


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  6 in total

1.  Computer simulations of the kinetics of irreversible enzyme inhibition by an unstable inhibitor.

Authors:  C M Topham
Journal:  Biochem J       Date:  1986-12-15       Impact factor: 3.857

2.  The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions.

Authors:  K Brocklehurst
Journal:  Biochem J       Date:  1979-09-01       Impact factor: 3.857

3.  Some classical errors in the kinetic analysis of enzyme reactions.

Authors:  K Brocklehurst; C M Topham
Journal:  Biochem J       Date:  1993-11-01       Impact factor: 3.857

4.  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

Review 5.  Kinetics of protein modification reactions.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1984-01-15       Impact factor: 3.857

6.  Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.

Authors:  K Brocklehurst; D Kowlessur; M O'Driscoll; G Patel; S Quenby; E Salih; W Templeton; E W Thomas; F Willenbrock
Journal:  Biochem J       Date:  1987-05-15       Impact factor: 3.857
  6 in total

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