Abstract
THE reconstitution of oligomeric enzymes from their denatured state is a consecutive process consisting of folding and association steps. In the case of multimeric enzymes the pathway of reassociation and its correlation with the occurrence of enzymatic activity is an open question. The combined use of crosslinking and SDS-polyacrylamide gel electrophoresis allows the assembly of multimeric enzymes to be followed quantitatively. We report here that by applying this technique to a study of lactic dehydrogenase from pig muscle, we have shown that tetramer formation parallels reactivation of the enzyme.
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HERMANN, R., RUDOLPH, R. & JAENICKE, R. Kinetics of in vitro reconstitution of oligomeric enzymes by cross-linking. Nature 277, 243–245 (1979). https://doi.org/10.1038/277243a0
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DOI: https://doi.org/10.1038/277243a0
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