One protein component corresponding to the γ
1-globulin fraction (γ
1-fraction) of bovine serum observed by cellulose acetate electorophoresis was recognized. This component (γ
1-component) formed a precipitation line which was detected on the cathode side of the transferrin precipitation line and on the anode side of the IgG precipitation line by immunoelectorophoresis with anti-bovine whole serum. It was contained in fractions dissolved with 0.06 M and 0.08 M phosphoric acid buffer solutions in DEAE-cellulose chromatography. The γ
1-component was precipitated after dialysis with distilled water. The crude γ
1-component still contained a Small amount of IgG. The γ
1-component was purified by removal of this IgG by the method of affinity choromatography using a Hormyl-Cellulofine-column (Seikagaku Kogyo Co., Ltd) combined with antibovine IgG. The γ
1-component was a protein other that the main proteins of IgG1, IgG2, IgM and IgA, which are contained in γ-globulin fractions. This suggested that the protein component is not one of the immuno-globulins corresponding to the γ
1-fraction of bovine serum and that γ
1-fraction may be formed more clearly as the component increases.
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