Studies on protein multimers. The association-dissociation behaviour of  -galactosidase in glycerol.
1. The effect of glycerol on the association-dissociation behaviour of beta-galactosidases from Escherichia coli is described. Two strains, K12 and ML308, were used as sources of enzyme. The conditions used, involving glycerol at a concentration of 90%, result in dissociation of the active 540000-dalton form to inactive structural subunits of 135000 daltons. 2. A pH-dependent process, assumed to be cyclic in mechanism, allows reassociation to an active form indistinguishable from the initial protein. 3. The apparently identical structural subunits, if produced in the presence of EDTA, were found to give rise to two electrophoretically distinguishable species. 4. Enzymes from both strains of E. coli can be distinguished electrophoretically but exhibit the same behaviour in glycerol. 5. A scheme of the association-dissociation is presented that is consistent with the behaviour observed and that has some predictive value.
D004492:Edetic Acid; D004589:Electrophoresis, Disc; D004926:Escherichia coli / Q000201:enzymology; D005696:Galactosidases; D005990:Glycerol; D006018:Glycols; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008956:Models, Chemical; D008970:Molecular Weight; D009905:Optical Rotatory Dispersion; D013053:Spectrophotometry; D014461:Ultracentrifugation
D006018:Glycols; D046911:Macromolecular Substances; D004492:Edetic Acid; D005696:Galactosidases; D005990:Glycerol