Macromolecular interaction and the electrophoretic mobility of esterase-5 from Drosophila pseudoobscura.
Esterase-5 is one of the most polymorphic loci in Drosophila pseudoobscura. Some variants reportedly produce a dimeric enzyme, while a few produce a monomeric form. This paper reports the finding that during electrophoresis ESTERASE-5 exists in a dynamic equilibrium between monomers and dimers, an equilibrium that is dependent on the running temperature of the gels. This is shown by a series of analytical electrophoresis experiments in which the apparent molecular weights of several variants are determined at four different temperatures. Increasing temperatures result in a linear decrease in the logarithm of apparent molecular weights. Macromolecular interactions thus are a significant determinant of EST-5 electrophoretic mobility.
D000818:Animals; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D014644:Genetic Variation; D008970:Molecular Weight; D011487:Protein Conformation; D013696:Temperature
D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase