GRZIWA, A and MAACK, S and PUHLER, G and WIEGAND, G and BAUMEISTER, W and JAENICKE, R (1994) DISSOCIATION AND RECONSTITUTION OF THE THERMOPLASMA PROTEASOME. EUROPEAN JOURNAL OF BIOCHEMISTRY, 223 (3). pp. 1061-1067. ISSN 0014-2956,
Full text not available from this repository.Abstract
The proteasome from the thermoacidophilic archaeon Thermoplasma acidophilum in its native state represents a 20S particle with significant secondary structure (approximate to 35% a helix) of its subunits. Electron microscopy, ultracentrifugal and spectral analysis demonstrate that at pH of less than 3 dissociation to partially denatured subunits occurs. Upon dialysis against near neutral pH buffers, at low protein concentration, reconstitution occurs, leading to the restoration of up to 90% of the native fluorescence signal. The recovery of activity depends on several parameters, including the buffer system, the pH used to dissociate the complex, and the duration of exposure to low pH. High concentrations of Ca2+ and Mg2+ cause partial dissociation of the Thermoplasma proteasome, yielding distinct subcomplexes. Neither the completely nor the partially dissociated complexes have proteolytic activity, indicating that function is linked to fully assembled proteasomes.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MULTICATALYTIC PROTEINASE; ACIDOPHILUM; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53160 |
Actions (login required)
 |
View Item |
