한국축산식품학회지 (Food Science of Animal Resources)

  • 제25권2호
  • /
  • Pages.232-237
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  • 2005
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  • 2636-0772(pISSN)
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  • 2636-0780(eISSN)
한국축산식품학회 (Korean Society for Food Science of Animal Resources)
권호 표지

저온에서 Rhodococcus erythropolis 균주로부터 재조합 젖소 Lactoferrin과 Lactoferrin N-lobe의 발현

Expression of Recombinant Bovine Lactoferrin and Lactoferrin N-lobe in Rhodococcus erythropolis at Low Temperature

  • 김완섭 (일본산업기술종합연구소 유전자발현공학연구실) ;
  • 김거유 (강원대학교 축산식품과학과) ;
  • 권일경 (강원대학교 축산식품과학과) ;
  • 고준수 (강원대학교 축산식품과학과)
  • Kim Woan-Sub (Proteolysis and Protein Turnover Research Group, Research Institute of Geonme-Based Biofactory, National Institute of Advanced Industrial Science and Technology(AIST)) ;
  • Kim Gur-Yoo (Department of Animal Food Science and Technology, Kangwon National University) ;
  • Kwon Ill-Kyung (Department of Animal Food Science and Technology, Kangwon National University) ;
  • Goh Juhn-Su (Department of Animal Food Science and Technology, Kangwon National University)
  • 발행 : 2005.06.01
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초록

락토페린은 트랜스페린 패밀리에 속하며, 철 결합성 당단백질로 대부분 포유동물의 젖에서 발견되고 있다 락토페린의 생리학적 기능으로는 항균활성, 항바이러스활성, 항염증반응, 항암효과, 세포의 성장과 항산화 효과 등이 알려져 있다. 본 연구는 PTip vector를 이용한 Rhodococcus erythropolis(R. erythropolis) 숙주로부터 재조합 젖소 락토페린과 락토페린 N-lobe의 생산을 시도하였다. 이들 단백질의 발현은 다양한 온도 범위에서 발현시켰다. 그리고 R. erythropolis의 숙주 내에서 이들 단백질의 발현은 낮은 온도 내에서도 가능함을 보여주었다. 생산된 재조합 단백질들은 Ni-NTA 정제 담체를 이용하여 정제하였다. 정제의 방법은 비변성 조건과 변성조건으로 수행하였다. 그리고 정제된 재조합 젖소 락토페린과 락토페린 N-lobe는 SDS-전기영동과 Western blot분석을 통하여 확인하였다. 생산된 재조합 젖소 락토페린은 분자량 80kDa, 그리고 락토페린 N-lobe가 43kDa의 분자량을 나타내었다.

Lactoferrin is a member of the transferrin family of iron-binding glycoproteins. It is originally found in milk. In addition to its antibacterial and antiviral activities, lactoferrin has many other biological functions include anti-inflammatory properties, antitumor, cell growth-promoting activity as well as antioxidant effect In the present study, we report the production of recombinant bovine lactoferrin and lactoferrin N-lobe in the Rhodococcus erythropolis (R erythropolis) using pTip vector. The expression level was investigated in various range of temperature, and we could successfully expressed the bovine lactoferrin and lactoferrin N-lobe in R erythropolis at low temperature. The recombinant proteins were purified by Nickel-Nitrolotriacetic acid (Ni-NTA). The purified proteins were confirmed by SDS-PAGE and Western blot, which indicating that the recombinant proteins have a molecular weight of 80kDa and 43kDa for bovine lactoferrin and lactoferrin N-lobe, respectively.

키워드

참고문헌

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