Circular dichroism of prophenol oxidase in relation to the structural stability in Drosophila melanogaster.
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.
Asada
Nobuhiko
N
Biological Laboratory, Faculty of Science, Okayama University of Science, Okayama, Japan. asada@das.ous.ac.jp
Namba
Masayoshi
M
Kodama
Takashi
T
Kyogoku
Yoshimasa
Y
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
D004792:Enzyme Precursors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase; D019840:2-Propanol