Earticle

초록

영어

Olfactory receptors, G protein-coupled receptor (GPCR), are integral membrane proteins composed of seven transmembrane spanning domains. These are not easy to be overexpressed, solubilized and purified because of their structures and strong hydrophobicity. Purification of olfactory receptor, where only a few studies have been done, is critical step for developing protein-based olfactory biosensor. In this work, human olfactory receptor, OR2AG1, was overexpressed in Escherichia coli. Electrophoresis of the overexpressed protein, visualized with Coomassie Blue staining and by immunoblotting with glutathione S-transferase (GST) antibody, revealed bands of 53, 118 and 160KDa, which were identified as the monomeric, dimeric and trimeric forms of the receptor proteins, respectively. The protein was difficult to solubilize with many detergents and only N-lauroyl sarcosine was found to be suitable for efficient solubilization. Human olfactory receptor, OR2AG1, was purified and solubilized by N-Lauroyl Sarcosine after treating membrane fraction with Triton X-100. Purified protein can be used as the primary transducer of olfactory biosensor after reconstitution in phospholipid vesicles.

키워드

저자

• Hyun Seok Song [ School of Chemical and Biological Engineering, Nano Bioelectronics & Systems Research Center, Seoul National University, Seoul, Korea ]
• Sang Hun Lee [ School of Chemical and Biological Engineering, Nano Bioelectronics & Systems Research Center, Seoul National University, Seoul, Korea ]
• Eun Hae Oh [ School of Chemical and Biological Engineering, Nano Bioelectronics & Systems Research Center, Seoul National University, Seoul, Korea ]
• Tai Hyun Park [ School of Chemical and Biological Engineering, Nano Bioelectronics & Systems Research Center, Seoul National University, Seoul, Korea ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576