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language
eng
Author
Yamamoto, Tatsuyuki Faculty of Life and Environmental Science, Shimane University
Takahashi, Tetsuya Faculty of Education, Shimane University
Description
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.
Subject
bovine pancreatic ribonuclease A
cyclodextrin
circular dichroism spectroscopy
fluorescence spectroscopy
inclusion
thermal stability
Journal Title
Journal of molecular structure
Volume
832
Start Page
96
End Page
100
ISSN
00222860
Published Date
2007-03-29
DOI
DOI Date
2013-04-01
NCID
AA00702852
Publisher
Elsevier
DCMI
text
NII Type
Journal Article
Format
PDF
Rights
Copyright c 2007 Elsevier B.V.
Text Version
著者版
OAI-PMH Set
Faculty of Life and Environmental Science
Faculty of Education
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