tailieunhanh - Báo cáo khoa học: Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase

Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) is a dual-func-tioning protein in the lipocalin family, acting as a PGD2-synthesizing enzyme and as an extracellular transporter for small lipophilic molecules. We earlier reported that denaturant-induced unfolding of L-PGDS follows a four-state pathway, including an activity-enhanced state and an inactive intermediate state. | ỊFEBS Journal Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase Tsukimi Iida1 Shigenori Nishimura2 Maki Mochizuki2 Susumu Uchiyama3 Tadayasu Ohkubo4 Yoshihiro Urade5 Akiyoshi Tanaka6 and Takashi Inui1 2 1 Department of Food and Nutrition Tsu City College Mie Japan 2 Graduate Schoolof Life and EnvironmentalSciences Osaka Prefecture University Japan 3 Department of Biotechnology Graduate Schoolof Engineering Osaka University Japan 4 Faculty of PharmaceuticalSciences Osaka University Japan 5 Department of Molecular BehavioralBiology Osaka Bioscience Institute Japan 6 Faculty of Bioresources Mie University Japan Keywords differential scanning calorimetry intermediate lipocalin L-PGDS thermal unfolding Correspondence T. Inui Department of Protein Sciences Graduate School of Life and Environmental Sciences Osaka Prefecture University 1-1 Gakuen-cho Naka-ku Sakai Osaka 599-8531 Japan Fax 81 72 254 9474 Tel 81 72 254 9473 E-mail inuit@ Received 6 September 2007 revised 12 November 2007 accepted 15 November 2007 doi Lipocalin-type prostaglandin PG D synthase L-PGDS is a dual-functioning protein in the lipocalin family acting as a PGD2-synthesizing enzyme and as an extracellular transporter for small lipophilic molecules. We earlier reported that denaturant-induced unfolding of L-PGDS follows a four-state pathway including an activity-enhanced state and an inactive intermediate state. In this study we investigated the thermal unfolding mechanism of L-PGDS by using differential scanning calorimetry DSC and CD spectroscopy. DSC measurements revealed that the thermal unfolding of L-PGDS was a completely reversible process at pH . The DSC curves showed no concentration dependency demonstrating that the thermal unfolding of L-PGDS involved neither intermolecular interaction nor aggregation. On the basis of a simple two-state unfolding mechanism the ratio of van t Hoff enthalpy AHv to calorimetric .

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