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Circular dichroism of prophenol oxidase in relation to the structural stability in Drosophila melanogaster
Author(s) -
Asada Nobuhiko,
Namba Masayoshi,
Kodama Takashi,
Kyogoku Yoshimasa
Publication year - 2004
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.10137
Subject(s) - drosophila melanogaster , circular dichroism , oxidase test , biology , denaturation (fissile materials) , biophysics , biochemistry , enzyme , chemistry , gene , nuclear chemistry
Circular dichroism (CD) of purified Drosophila melanogaster prophenol oxidase has been measured in the range of 195–245 nm. So far, few investigations about the interaction on higher‐order structures have been performed. CD spectra of Drosophila prophenol oxidase with 2‐propanol activator showed fluctuation of α‐helices. At a high temperature of 80°C, prophenol oxidase was partially denatured. However, it showed reversible recovery by renaturation after returning to low temperature at 30°C. The conformational changes and reversible denaturation‐renaturation interaction of the prophenol oxidase protein are discussed. Arch. Insect Biochem. Physiol. 56:1–6, 2004. © 2004 Wiley‐Liss, Inc.