Renaturation of acid-denatured rabbit muscle aldolase. Existence and properties of a stable monomeric intermediate.
The effects of temperature, pH and the substrate, fructose 1,6-bisphosphate, upon the kinetics and yield of renaturation of acid-denatured rabbit muscle aldolase have been investigated. The results are discussed in terms of a sequential set of events leading from the unfolded polypeptide chain to the renatured oligomeric enzyme. One of the intermediate molecular species in this sequence has been characterized as a folded monomer with a sedimentation coefficient of 3.1 S. This monomer is shown to be much more heat-labile than the tetramer under identical conditions, thus demonstrating stabilization of the tertiary structure of the polypeptide chain by the quaternary interactions between protomers.
D000818:Animals; D001665:Binding Sites; D002499:Centrifugation, Density Gradient; D003460:Crystallization; D003956:Dialysis; D004355:Drug Stability; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005636:Fructosephosphates; D006598:Hexosediphosphates; D006358:Hot Temperature; D007700:Kinetics; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D011489:Protein Denaturation; D011817:Rabbits; D013997:Time Factors
D005636:Fructosephosphates; D006598:Hexosediphosphates; D046911:Macromolecular Substances; D005634:Fructose-Bisphosphate Aldolase