title: Circular dichroism of prophenol oxidase in relation to the structural stability in Drosophila melanogaster.
abstract: 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 alpha-helices. At a high temperature of 80 degrees C, prophenol oxidase was partially denatured. However, it showed reversible recovery by renaturation after returning to low temperature at 30 degrees C. The conformational changes and reversible denaturation-renaturation interaction of the prophenol oxidase protein are discussed.
authors.affiliation: Biological Laboratory, Faculty of Science, Okayama University of Science, Okayama, Japan. asada@das.ous.ac.jp
authors.forename: Nobuhiko
authors.initials: N
authors.lastname: Asada
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Namba
authors.forename: Takashi
authors.initials: T
authors.lastname: Kodama
authors.forename: Yoshimasa
authors.initials: Y
authors.lastname: Kyogoku
mesh_terms: D019840:2-Propanol / Q000494:pharmacology; D000818:Animals; D004156:Catechol Oxidase / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D004331:Drosophila melanogaster / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D004792:Enzyme Precursors / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D011487:Protein Conformation; D013696:Temperature
chemical_list: D004792:Enzyme Precursors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase; D019840:2-Propanol