help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 41: 23-28 (1983)
© 1983 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vincent, J C
Right arrow Articles by Thellier, M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vincent, J C
Right arrow Articles by Thellier, M

Theoretical analysis of the significance of whether or not enzymes or transport systems in structured media follow Michaelis-Menten kinetics.

J C Vincent and M Thellier

ABSTRACT

Pure Michaelis-Menten enzymes have been studied (i.e., enzymes with a hyperbolic (S, V) behavior in a well-stirred solution). When such enzymes are associated with a structure in vitro, even in the simplest conceivable form (immobilization in a homogeneous gel), they can produce enzymic or transport reactions with many different kinetics (Michaelis-Menten, sigmoidal, dual-phasic, etc.). Therefore, when structured enzyme or transport processes in vivo have sigmoidal kinetics, it is not proof that the corresponding proteins are allosteric. In same manner, when the apparent kinetics are dual-phasic, it is not proof that two enzyme, or transport systems, coexist.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1983 by the Biophysical Society.