Literature DB >> 2948570

Kinetic characterization of an enzymatic irreversible inhibition measured in the presence of coupling enzymes. The inhibition of adenosine triphosphatase from sarcoplasmic reticulum by fluorescein isothiocyanate.

J A Teruel, J Tudela, F Fernández Belda, F García Carmona, J C Gómez Fernández, F García Cánovas.   

Abstract

A kinetic study of the irreversible inhibition of an enzyme measured in the presence of a coupling enzyme system has been carried out to assess the type of mechanism of the irreversible inhibition. By using the algebraic criteria proposed here it should be possible to discriminate between these mechanisms and to calculate their corresponding kinetic constants. An experimental design has been developed and applied to fluorescein isothiocyanate as inhibitor of the ATPase activity from sarcoplasmic reticulum.

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Year:  1987        PMID: 2948570     DOI: 10.1016/0167-4838(87)90016-1

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


  4 in total

1.  Kinetic differentiation between enzyme inactivation involving complex-formation with the inactivator and that involving a conformation-change step.

Authors:  C Liu; C L Tsou
Journal:  Biochem J       Date:  1992-03-01       Impact factor: 3.857

2.  Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid.

Authors:  M H Wang; Z X Wang; K Y Zhao
Journal:  Biochem J       Date:  1996-11-15       Impact factor: 3.857

3.  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

4.  Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis.

Authors:  M J Navarro-Lozano; E Valero; R Varon; F Garcia-Carmona
Journal:  Bull Math Biol       Date:  1995-01       Impact factor: 1.758

  4 in total

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