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KMID : 0380619970290051067
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Korean Journal of Food Science and Technology
1997 Volume.29 No. 5 p.1067 ~ p.1070
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An Effective Method of Isolating Immunoglobulins from Bovine Plasma Proteins
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Choi In-Wook
Lee Hyun-Jung
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Abstract
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Imunoglobulins from bovine plasma proteins were isolated by IMAC which Cu^(2+) was Chelated on a chelating sepharose fast flow gel. Most plasma proteins were eluted by 1st (0.01 M Na₂HPO₄, 0.5 M NaCl, pH 4.0) and 2nd elution buffers (0.01 M imidazol). According to the reverse phase HPLC analysis, it was found that proteins which were eluted by 1st elution buffer were mainly composed of serum albumin, while most IgG and transferrin were eluted by 2nd elution buffer. When protein fractions obtained by 2nd elution buffer was applied to ultra filtration system (molecular weight cut off: 100 kD), IgG was further purified. These results indicate that IMAC is an excellent tool for isolating imunoglobulins from plasma proteins.
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