Stretched-exponential analysis of heat-induced aggregation of apo-concanavalin A.
The kinetics of heat-induced aggregation of apo-concanavalin A (aConA) was investigated as a function of temperature and protein concentration by circular dichroism and turbidity. Heat-induced aggregation, as well as conformational change, of aConA was fitted to stretched-exponential equations. The exponent of the conformational change maintained 0.5 despite the protein concentration and temperature, indicating the presence of a common intermediate during the conformational change. After the process, aggregates grew with increasing temperature and initial protein concentration. The reaction order of aggregation was 1.5, indicating that the rate-limiting steps of aConA aggregation involve both conformational change and aggregation.
Kudou
Motonori
M
School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan.
Shiraki
Kentaro
K
Takagi
Masahiro
M
D001059:Apoproteins / Q000737:chemistry*; D003208:Concanavalin A / Q000737:chemistry*; D003627:Data Interpretation, Statistical; D006358:Hot Temperature; D011487:Protein Conformation
D001059:Apoproteins; C048717:apoconcanavalin A; D003208:Concanavalin A