Yoshikiyo1.pdf 137 KB
Yamamoto, Tatsuyuki Faculty of Life and Environmental Science, Shimane University
Takahashi, Tetsuya Faculty of Education, Shimane University
Circular dichroism and fluorescence spectroscopic measurements showed that the thermal denaturation and renaturation processes of bovine pancreatic ribonuclease A (RNase A) in an aqueous solution at pH 7.0 are greatly affected by the addition of glucosyl-β-cyclodextrin (G1-β-CD). The result of circular dichroism measurements revealed that G1-β-CD lowered the thermal stability of RNase A to result in an irreversible denaturation of RNase A in the aqueous solution. The α- and γ-cyclodextrin gave less effect on the thermal stability. The ellipticity at 220 nm of the thermally denatured RNase A scarcely recovered with the re-cooling process in the presence of G1-β-CD. The temperature dependency of the fluorescence intensity at 309 nm due to six tyrosine residues of RNase A was significantly affected by the addition of G1-β-CD. The effect of the addition of CDs on the thermal stability was larger in the order of G1-β-CD > γ-CD > α-CD.
bovine pancreatic ribonuclease A
circular dichroism spectroscopy
Journal of molecular structure
Copyright c 2007 Elsevier B.V.
Faculty of Life and Environmental Science
Faculty of Education