Literature DB >> 5047703

Dalziel rate behaviour in ternary-complex mechanisms for enzyme reactions involving two substrates.

G Pettersson.   

Abstract

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Year:  1972        PMID： 5047703     DOI： 10.1016/0005-2744(72)90002-2

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


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  6 in total

1.  Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase.

Authors:  F M Dickinson; C J Dickenson
Journal:  Biochem J       Date:  1978-06-01       Impact factor: 3.857

2.  A kinetic analysis of enzyme systems involving four substrates.

Authors:  K R Elliott; K F Tipton
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

3.  The regulatory properties of rabbit muscle pyruvate kinase. The influence of substrate concentrations.

Authors:  S Ainsworth; J Kinderlerer; R B Gregory
Journal:  Biochem J       Date:  1983-02-01       Impact factor: 3.857

4.  Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols.

Authors:  W Schöpp; H Aurich
Journal:  Biochem J       Date:  1976-07-01       Impact factor: 3.857

5.  Ligand binding on to maize (Zea mays) malate synthase: a structural study.

Authors:  S Beeckmans; A S Khan; L Kanarek; E Van Driessche
Journal:  Biochem J       Date:  1994-10-15       Impact factor: 3.857

6.  Kinetic studies of the mechanism of pig kidney aldehyde reductase.

Authors:  F F Morpeth; F M Dickinson
Journal:  Biochem J       Date:  1981-02-01       Impact factor: 3.857
  6 in total

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