Table 1. Parameters of thermal denaturation and aggregation of bovine serum albumin ([BSA] = 1 mg/ml, 0.1 M Na-phosphate buffer, pH 7.0).
T, °C | , min | γnon-agg,lim | γUhr | γUlr,agg | Rh,1, nm | Rh,2, nm | I2, counts/s |
---|---|---|---|---|---|---|---|
60 | 19±1 | 0.51±0.01 | γUhr + γUlr,agg = 0.49±0.01 | – | 11.1±0.1 | (3.2±0.1)∙103 | |
65 | 13.6±0.6 | 0.35±0.01 | 0.51±0.03 | 0.14±0.03 | 10.3±0.3 | 12.8±0.3 | (5.1±0.1)∙103 |
70 | 1.6±0.1 | 0.05±0.01 | γUhr + γUlr,agg = 0.95±0.01 | 10.4±0.4 | 15.1±0.4 | (12.1±0.1)∙103 | |
80 | 1.5±0.1 | 0.06±0.01 | γUhr + γUlr,agg = 0.94±0.01 | – | – | – |
Designations: is the time of half-conversion for the kinetic curves of BSA denaturation, γnon-agg,lim is the portion of the unfolded protein that remains unincorporated in the large-sized aggregates for a long time (this species corresponds to Ast in Fig 6), γUhr is the portion of the highly reactive unfolded form, γUlr,agg is the portion of the low reactive unfolded form that is involved in the aggregation process by the attachment to the primary aggregates, I2 is the value of the light scattering intensity reached after completion of the formation of the secondary aggregates, Rh,1 and Rh,2 are the hydrodynamic radius of the primary and the secondary aggregates, respectively.