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KMID : 1024620050250020232
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Food Science of Animal Resources
2005 Volume.25 No. 2 p.232 ~ p.237
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Expression of Recombinant Bovine Lactoferrin and Lactoferrin N-lobe in Rhodococcus erythropolis at Low Temperature
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Kim Woan-Sub
Kim Gur-Yoo
Kwon Il-Kyoung
Goh Juhn-Su
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Abstract
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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.
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KEYWORD
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lactoferrin, milk protein, Rhodococcus
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