Open AccessReconstitution of the Allosteric l ‐Lactate Dehydrogenase from Lactobacillus casei Investigated by Hybridization
Author(s) -
MAYR Ulrich,
HENSEL Reinhard,
KANDLER Otto,
PRUSCHA Helmut
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05239.x
Subject(s) - lactobacillus casei , allosteric regulation , lactate dehydrogenase , tetramer , chemistry , enzyme , biochemistry , dehydrogenase , lactic dehydrogenase , fermentation
The reassociation process of the urea‐denatured allosteric l ‐lactate dehydrogenase from Lactobacillus casei was investigated by hybridization experiments between the reassociating enzymes from L. casei and Lactobacillus curvatus . The quantitatively evaluated hybridization patterns indicate an assembly pathway from the unfolded subunits to the tetrameric state via dimers. The comparison of the kinetics of reassociation and reactivation of the L. casei l ‐lactate dehydrogenase shows that the tetramer is the only active form.