TY  - JOUR
AU  - Ghahghaei, Arezou 
PY  - 2008
TI  - The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin
JF  - American Journal of Biochemistry and Biotechnology
VL  - 4
IS  - 4
DO  - 10.3844/ajbbsp.2008.317.324
UR  - https://thescipub.com/abstract/ajbbsp.2008.317.324
AB  - Aggregation of beta-lactoglobulin occurs mainly via intermolecular disulphide bond exchange. Upon heating, beta-lactoglobulin aggregated which increased with increasing pH. The presence of DTT led to more rapid aggregation and precipitation of beta-lactoglobulin. Alpha-Crystallin prevented the aggregation of heat-stressed beta-lactoglobulin and was a more efficient chaperone at higher pH values. In the presence of DTT, however, alpha-crystallin was a less efficient chaperone due to faster aggregation of heated and reduced beta-lactoglobulin.