Stability and Refolding of Prophenol Oxidase Protein with 2-Propanol in Drosophila melanogaster  

作　　者：Eri Sato Kotomi Mita Nobuhiko Asada 

机构地区：[1]Department of Zoology, Faculty of Science, Okayama University of Science, Kita-ku, Okayama 700-0005, Japan [2]Graduate School of Systems Life Sciences, Kyusyu University, Higashi-ku, Fukuoka 812-8581, Japan

出　　处：《Journal of Life Sciences》2012年第8期952-956,共5页生命科学（英文版）

摘　　要：Phenol oxidase in Drosophila melanogaster occurs as folded phase precursors designated as prophenol oxidase A1 and A3, and prophenol oxidase is activated with alcohol, especially 2-propanol, within a few minutes as unfolded-phase in vitro. To clarify a common effect of alcohols on proteins and peptides, the extract containing prophenol oxidase protein was prepared. Phenol oxidase activity activated with 2-propanol has been maintained stable at least 24 hours remains as it is. Protein of prophenol oxidase was not denatured opposite hypnoses known as the instability of protein with alcohol. Activated prophenol oxidase with 2-propanol remain enzyme activity with no aggregation, stable, renaturation, and the refolding phenomena occurred around the active phase within the catalytic active center of prophenol oxidase protein in Drosophila melanogaster. This study is important to induce the wide range applications of the effect in many fields for rational drag design.

关 键 词：STABILITY 2-propanol REFOLDING prophenol oxidase Drosophila melanogaster. 

分 类 号：Q959.223.5[生物学—动物学] Q969.462.2