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ABSTRACT
Destabilization of Lysozyme and chaperone like action of alpha crystallin isolated from goat’s eye lens was investigated at various temperature ranges in phosphate buffer (pH 7.1) solution and dithiothretol (DTT). This was monitored spectrophotometrically at 260nm. The heat and DTT-induced destabilization of lysozyme was prevented by alpha crystallin in a concentration dependent manner. Alpha crystallin like other chaperones, fulfils its chaperone like action in preventing aggregation of denatured proteins by the formation of complexes
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