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. Author manuscript; available in PMC: 2014 May 28.
Published in final edited form as: Biochemistry. 2013 May 16;52(21):10.1021/bi301662w. doi: 10.1021/bi301662w

Table 1.

Stability of the peptide-protein complexes in dissociating agentsa

Dissociating Agents Protein recovered in soluble fraction ( % of total)b
Phosphate buffer (PBS) 0.01
PBS – 1% Tween-20 0.012
PBS-1% Triton X-100 12
1 M NaCl 0.001
2M MgCl2 0.001
8 M Urea 62
1% SDS 12
6 M Guanidium Hydrochloride 68
a

α-crystallin and αA66-80 peptide (2:1) ratio (W/W) were incubated at 37°C for 18 h. After incubation, the samples were centrifuged (10,000 g, 10 min) and the aggregates were resuspended in different dissociating agents and placed in roller shaker at 37°C for 1 h. The samples were again centrifuged at 8000 rpm for 10 min. Protein content of the supernate was estimated by Bio-Rad protein assay. Protein content of the sample at 0 min before incubation was taken as 100%.

b

Bold-faced percentages indicate the maximum solubility of the aggregate in 8 M urea and 6 M guanidium hydrochloride