Open AccessRenaturation of Acid‐Denatured Rabbit Muscle Aldolase
Author(s) -
VIMARD Christian,
ORSINI Gilbert,
GOLDBERG Michel E.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb03952.x
Subject(s) - tetramer , aldolase a , monomer , protein quaternary structure , chemistry , kinetics , enzyme , sedimentation coefficient , biochemistry , substrate (aquarium) , yield (engineering) , fructose , stereochemistry , sequence (biology) , crystallography , biology , organic chemistry , polymer , materials science , ecology , physics , protein subunit , quantum mechanics , gene , metallurgy
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.