Abstract:
Destabilization of Lysozyme
and chaperone
like
action of alpha crystallinisolated 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.
