Bernhardt, Günther and Rudolph, Rainer and Jaenicke, Rainer (1981) Reassociation of lactic dehydrogenase from pig heart studied by cross-linking with glutaraldehyde. Zeitschrift fuer Naturforschung, C Journal of Biosciences 36C (9-10), pp. 772-777.
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Crosslinking with glutaraldehyde was applied to the study of the assembly of lactate dehydrogenase from pig heart. To eliminate perturbations caused by excessive folding reactions, acid dissocn. was performed in the presence of 0.8M Na2SO4 at 0 Deg. Under optimum conditions complete crosslinking of the tetrameric enzyme was achieved in <2 min. Crosslinking during reconstitution proves the dimer to be the only intermediate of reassocn.. The dimer-tetramer transition is rate-limiting for both reassocn. and reactivation, suggesting the tetramer to be the enzymically active species. The presence of monomers during reconstitution indicates that tetramer formation is preceded by a fast monomer-dimer equil. The kinetic model describing the exptl. data is: 4 monomers .dblharw. 2 dimers (with equil. const. K) and 2 dimers -> 1 tetramer (with a 2nd-order rate const. k). K Was 3 * 107 L mol-1, and k was 1.4 * 104 L mol-1.
|Additional information (public):||CAN 95:217064 7-5 Enzymes 9001-60-9 Role: BIOL (Biological study) (subunit assembly of, kinetics of, of heart)|
|Institutions:|| Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer) |
Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
|Keywords:||Heart, composition (lactate dehydrogenase of, subunit assembly of); Kinetics, reaction (of lactate dehydrogenase subunit assembly); Molecular association (of lactate dehydrogenase subunits, kinetics of); lactate dehydrogenase subunit assembly|
|Subjects:||500 Science > 570 Life sciences|
500 Science > 540 Chemistry & allied sciences
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||15 Jan 2009 17:24|
|Last Modified:||05 Aug 2009 15:50|
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