Literature DB >> 1198092

The quantitative relations between diffusion-controlled reaction rate and characteristic parameters in enzyme-substrate reactions systems. II. Charged substrates.

C Kuo-chen, K Chih-kun.   

Abstract

The quantitative relationship between the spatial factor and the force-range factor on the one hand and the ionic strength and the charges of reactants on the other has been calculated for non-spherically symmetric reaction systems. New upper limits of combination reactions between enzymes and charged substrates have been obtained. Applying the calculated results to the reactions catalyzed by fumarase and D-glyceraldehyde-3 phosphate dehydrogenase, we have been able to interpret experimental phenomena which could not be accounted for by the conventional theory of the diffusion-controlled reaction. Furthermore, the conditions under which the Bronsted equation is valid in the non-equilibrium steady state reaction system have been discussed.

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Year:  1975        PMID: 1198092

Source DB:  PubMed          Journal:  Sci Sin        ISSN: 0250-7870


  2 in total

1.  A consideration of the effects of added solutes on the activity of bovine superoxide dismutase.

Authors:  M E McAdam
Journal:  Biochem J       Date:  1977-03-01       Impact factor: 3.857

2.  Acetylcholinesterase: evidence that sodium ion binding at the anionic site causes inhibition of the second-order hydrolysis of acetylcholine and a decrease of its pKa as well as of deacetylation.

Authors:  H R Smissaert
Journal:  Biochem J       Date:  1981-07-01       Impact factor: 3.857

  2 in total

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