• Food Science of Animal Resources
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• v.20 no.2
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• pp.125-132
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• 2000

Lactoferrin was isolated from the colostrum of Korean native cow by using several purification steps such as batch extraction, ion exchange chromatography, gel filtration chromatography and affinity chromatography. Other whey protein components that having similar molecular weight and affinity to lactoferrin were gradually removed from crude Korean native cow's lactoferrin during the purification steps. The amount of lactoferrin collected from a liter of Korean native cow's colostrum was 65mg and the recovery rate was 29.4%. The molecular weight of the purified Korean native cow's lactoferrin was estimated approximately 81,000dalton.

• Journal of Dairy Science and Biotechnology
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• v.23 no.1
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• pp.1-8
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• 2005

The purpose of this study was to demonstrate biochemical properties and antibacterial activity of lactoferrin(Lf) obtained from the colostrum of Korean native cow. Lactoferrin was isolated from the colostrum of Korean native cow by purification steps using batch extraction, ion exchange chromatography, gel filtration chromatography, affinity chromatography. Other whey protein components that is similar molecular weight and affinity to lactoferrin were gradually removed from crude Korean Native cow's lactoferrin during the purification steps. The molecular weight of the purified Korean native cow's Lf(K-Lf) was 81 kDa, the isoelectric point was 9, and the content of iron was 0.56mg/g, which is indicated that iron saturation of the K-Lf was 40.6%. Amino acid composition and a-helix content were different K-Lf from bovine Lf(B-Lf). Antibacterial activity of E. coli O111 by K-Lf was lower than that of B-Lf. A minimal inhibitory concentration(MIC) of K-Lf and B-Lf was 2.75mg/ml and 1.5mg/ml respectively.

• Food Science of Animal Resources
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• v.25 no.1
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• pp.98-102
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• 2005

The purpose of this study was to demonstrate biochemical properties of lactoferrin (Lf) obtained from the colostrum of Korea native cow. The molecular weight of the purified Korean native cow's Lf (K-Lf) was 81kDa, the isoelectric point was 9, and the content of iron was 0.56 mg/g, which is indicated that iron saturation of the lactoferrin was 40.6%. Amino acid composition and a-helix content were different K-Lf from bovine Lf (B-Lf). Immunological cross reactivity was observed between K-Lf and B-Lf but not between K-Lf and human Lf (H-Lf) by immunodiffusion test and Western blot analysis. Out results indicate that structure of K-Lf is different from that of B-Lf although K-Lf and B-Lf were immunologically cross-reactive.

• Journal of Animal Science and Technology
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• v.48 no.4
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• pp.595-602
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• 2006

The purpose of this study is to demonstrate antimicrobial activities of the lactoferrin and its peptic hydrolysates obtained from the colostrums of Hanwoo(Korean native cattle) and Holstein cattle. In the measurement of antimicrobial activity to E. coli O111 and other microorganisms, bovine lactoferrin showed a higher antimicrobial activity than that of Hanwoo cow's lactoferrin . The minimal inhibitory concentration (MIC) of lactoferrin against E. coli O111 was exhibited 1.5mg/ml(Holstein) and 2.75mg/ml (Hanwoo). The same result was also observed between bovine lactoferrin hydrolysate (0.12mg/ml) and Hanwoo cow's lactoferrin hydrolysate (0.25mg/ml). In addition of lysozyme, antimicrobial activity of lactoferrin was increased.