Biological processes in organised media.
Embedding a simple Michaelis-Menten enzyme in a gel slice may allow the catalysis of not only scalar processes but also vectorial ones, including uphill transport of a substrate between two compartments, and may make it seem as if two enzymes or transporters are present or as if an allosterically controlled enzyme/transporter is operating. The values of kinetic parameters of an enzyme in a partially hydrophobic environment are usually different from those actually measured in a homogeneous aqueous solution. This implies that fitting kinetic data (expressed in reciprocal co-ordinates) from in vivo studies of enzymes or transporters to two straight lines or a sigmoidal curve does not prove the existence of two different membrane mechanisms or allosteric control. In the artificial transport systems described here, a functional asymmetry was sufficient to induce uphill transport, therefore, although the active transport systems characterised so far correspond to proteins asymmetrically anchored in a membrane, the past or present existence of structurally symmetrical systems of transport in vivo cannot be excluded. The fact that oscillations can be induced in studies of the maintenance of the electrical potential of frog skin by addition of lithium allowed evaluation of several parameters fundamental to the functioning of the system in vivo (e.g., relative volumes of internal compartments, characteristic times of ionic exchanges between compartments). Hence, under conditions that approach real biological complexity, increasing the complexity of the behaviour of the system may provide information that cannot be obtained by a conventional, reductionist approach.
Thellier
Michel
M
Laboratoire des Processus intégratifs cellulaires, faculté des sciences, université de Rouen, 76821 Mont-Saint-Aignan, France. Michel.Thellier@univ-rouen.fr
Vincent
Jean-Claude
JC
Alexandre
Stéphane
S
Lassalles
Jean-Paul
JP
Deschrevel
Brigitte
B
Norris
Victor
V
Ripoll
Camille
C
D000494:Allosteric Regulation; D000818:Animals; D001001:Anura; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004848:Epithelium / Q000187:drug effects / Q000502:physiology; D005782:Gels; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008094:Lithium / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D008564:Membrane Potentials / Q000187:drug effects; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D012995:Solubility
D002352:Carrier Proteins; D004800:Enzymes, Immobilized; D005782:Gels; D008094:Lithium; D000254:Sodium-Potassium-Exchanging ATPase; D008274:Magnesium