We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Effect of α-crystallin on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle.
- Authors
Meremyanin, A.; Eronina, T.; Chebotareva, N.; Kleimenov, S.; Yudin, I.; Muranov, K.; Ostrovsky, M.; Kurganov, B.
- Abstract
Thermal aggregation of rabbit skeletal muscle glycogen phosphorylase b (Ph b) has been investigated using dynamic light scattering under conditions of a constant rate of temperature increase (1 K/min). The linear behavior of the dependence of the hydrodynamic radius on temperature for Ph b aggregation is consistent with the idea that the rmal aggregation of proteins proceeds in the kinetic regime where in the rate of aggregation is limited by diffusion of the interacting particles (the regime of “diffusion-limited cluster-cluster aggregation”). In the presence of α-crystallin, a prote in exhibiting chaperone-like activity, the dependence of the hydrodynamic radius on temperature follows the exponential law; this suggests that the aggregation process proceeds in the kinetic regime where the sticking probability for colliding particles becomes lower than unity (the regime of “reaction-limited cluster-cluster aggregation”). Based on analysis of the ratio between the light scattering intensity and the hydrodynamic radius of Ph b aggregates, it has been concluded that the addition of α-crystallin results in formation of smaller size starting aggregates. The data on differential scanning calorimetry indicate that α-crystallin interacts with the intermediates of the unfolding process of the Ph b molecule. The proposed scheme of the rmal denaturation and aggregation of Ph b includes the stage of reversible dissociation of dimers of Ph b into monomers, the stage of the formation of the starting aggregates from the denatured monomers of Ph b, and the stage of the sticking of the starting aggregates and higher order aggregates. Dissociation of Ph b dimer into monomers at elevated temperatures has been confirmed by analytical ultracentrifugation.
- Subjects
GLYCOGEN phosphorylase; HYDRODYNAMICS; DIFFUSION; MONOMERS; MUSCLES; BIOCHEMISTRY
- Publication
Biochemistry (00062979), 2007, Vol 72, Issue 5, p518
- ISSN
0006-2979
- Publication type
Article
- DOI
10.1134/S0006297907050082