| | 1 | Author
| Stefan Zabori, Rainer Rudolph, Rainer Jaenicke | Requires cookie* | | | Title
| Folding and Association of Triose Phosphate Isomerase from Rabbit Muscle  | | | | Abstract
| The enzymatic activity and quaternary structure o f rabbit muscle triose phosphate isomerase remains unchanged in the concentration range from 2 ng/m l to 2 ng/m l. In this concentration range the enzyme can be reactivated after dissociation and denaturation in 6.5 m guanidine hydrochloride. Removal of the denaturant by dilution and separation o f inactive wrong aggregates (5-20%) lead back to active dimers, indistinguishable from the native enzyme as far as enzymatic and physicochemical properties are concerned. Based on the long term stability o f the enzyme, the reactivation kinetics were analyzed at low concentrations and 0 °C, conditions where the association of inactive monomers to active dim ers is predom inant in the process of reactivation. The concentration dependence of the rate of reactivation and the kinetic profiles could be described by a consecutive first-order folding and second-order association reaction scheme with the rate constants k ^ = 1.9 x 10~2 s-1 and kbi = 3 x 105 m _1 • s~\ This implies that the folded monomers o f triose phosphate isomerase, which are interm ediate states during reconstitution, cannot possess appreciable enzymatic | | | |
Reference
| Z. Naturforsch. 35c, 999—1004 (1980); received A ugust 7 1980 | | | |
Published
| 1980 | | | |
Keywords
| Association, Folding, Reconstitution, Triose Phosphate Isomerase | | | |
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| default:Reihe_C/35/ZNC-1980-35c-0999.pdf | | | | Identifier
| ZNC-1980-35c-0999 | | | | Volume
| 35 | |
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