The Effects of Cyclodextrins on the Thermal Denaturation and Renaturation Processes of Bovine Pancreatic Ribonuclease A in an Aqueous Solution Studied by Circular Dichroism and Fluorescence Spectroscopy.

Journal of molecular structure Volume 832 Page 96-100 published_at 2007-03-29
アクセス数 : 1602
ダウンロード数 : 96

今月のアクセス数 : 76
今月のダウンロード数 : 2
File
Yoshikiyo1.pdf 137 KB エンバーゴ : 2007-05-21
Title
The Effects of Cyclodextrins on the Thermal Denaturation and Renaturation Processes of Bovine Pancreatic Ribonuclease A in an Aqueous Solution Studied by Circular Dichroism and Fluorescence Spectroscopy.
Creator
Source Title
Journal of molecular structure
Volume 832
Start Page 96
End Page 100
Journal Identifire
ISSN 00222860
Descriptions
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.
Subjects
bovine pancreatic ribonuclease A ( Other)
cyclodextrin ( Other)
circular dichroism spectroscopy ( Other)
fluorescence spectroscopy ( Other)
inclusion ( Other)
thermal stability ( Other)
Language
eng
Resource Type journal article
Publisher
Elsevier
Date of Issued 2007-03-29
Rights
Copyright c 2007 Elsevier B.V.
Publish Type Accepted Manuscript
Access Rights open access
Relation
[DOI] 10.1016/j.molstruc.2006.08.007
[NCID] AA00702852