@article {10.3844/ajbbsp.2008.317.324,
article_type = {journal},
title = {The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin},
author = {Ghahghaei, Arezou},
volume = {4},
number = {4},
year = {2008},
month = {Dec},
pages = {317-324},
doi = {10.3844/ajbbsp.2008.317.324},
url = {https://thescipub.com/abstract/ajbbsp.2008.317.324},
abstract = {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.},
journal = {American Journal of Biochemistry and Biotechnology},
publisher = {Science Publications}
}