Fig. 3C shows migration of the purified VhChiP to above 95 kDa, corresponding to the trimeric form, when unheated (lane 1).
The trimer remained intact when the temperature was raised to 40°C, but began to dissociate at 50°C. At 60°C, more than half of the VhChiP trimers were dissociated to monomers and at 70°C or above, no trimers remained. These results indicate that VhChiP is a heat-sensitive, SDS-stable trimer; each subunit has apparent MW of approximately 39 kDa, consistent with the predicted MW of the translated polypeptide lacking the signal sequence.