Tags

Type your tag names separated by a space and hit enter

Stability of ribonuclease T2 from Aspergillus oryzae.
Protein Sci. 1995 Mar; 4(3):416-20.PS

Abstract

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.mol-1 at 25 degrees C by linear extrapolation method. From the thermal unfolding experiment in 20 mM sodium phosphate buffer at pH 7.5, the Tm and the enthalpy change of RNase T2 were found to be 55.3 degrees C and 119.1 kcal.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.

Authors+Show Affiliations

Department of Biology, Faculty of Science, Osaka University, Japan.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7795525

Citation

Kawata, Y, and K Hamaguchi. "Stability of Ribonuclease T2 From Aspergillus Oryzae." Protein Science : a Publication of the Protein Society, vol. 4, no. 3, 1995, pp. 416-20.
Kawata Y, Hamaguchi K. Stability of ribonuclease T2 from Aspergillus oryzae. Protein Sci. 1995;4(3):416-20.
Kawata, Y., & Hamaguchi, K. (1995). Stability of ribonuclease T2 from Aspergillus oryzae. Protein Science : a Publication of the Protein Society, 4(3), 416-20.
Kawata Y, Hamaguchi K. Stability of Ribonuclease T2 From Aspergillus Oryzae. Protein Sci. 1995;4(3):416-20. PubMed PMID: 7795525.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stability of ribonuclease T2 from Aspergillus oryzae. AU - Kawata,Y, AU - Hamaguchi,K, PY - 1995/3/1/pubmed PY - 1995/3/1/medline PY - 1995/3/1/entrez SP - 416 EP - 20 JF - Protein science : a publication of the Protein Society JO - Protein Sci VL - 4 IS - 3 N2 - 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.mol-1 at 25 degrees C by linear extrapolation method. From the thermal unfolding experiment in 20 mM sodium phosphate buffer at pH 7.5, the Tm and the enthalpy change of RNase T2 were found to be 55.3 degrees C and 119.1 kcal.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. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/7795525/Stability_of_ribonuclease_T2_from_Aspergillus_oryzae_ L2 - https://doi.org/10.1002/pro.5560040308 DB - PRIME DP - Unbound Medicine ER -