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Protein Science, Vol 4, Issue 3 416-420, Copyright © 1995 by Cold Spring Harbor Laboratory Press

ARTICLE

Stability of ribonuclease T2 from Aspergillus oryzae

Y. KAWATA and K. HAMAGUCHI
Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680, Japan

The stability of ribonuclease T2 (RNase T2) from Aspergillus oryzae against guanidine hydrochloride and heat was studied by using CD and fluorescence. RNase T2 unfolded and refolded reversibly concomitant with activity, but the unfolding and refolding rates were very slow (order of hours). The free energy change for unfolding of RNase T2 in water was estimated to be 5.3 kcal{middot}mol(-1) at 25{deg}C by linear extrapolation method. From the thermal unfolding experiment in 20 mM sodium phosphate buffer at pH 7.5, the T(m) and the enthalpy change of RNase T2 were found to be 55.3{deg}C and 119.1 kcal{middot}mol(-1), respectively. From these equilibrium and kinetic studies, it was found that the stability of RNase T2 in the native state is predominantly due to the slow rate of unfolding.
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