Albumin fraction was purified from the swamp eel by salting out with ammonium sulfate and following by DEAE-Sephadex A50 column chromatography. The purified albumin fraction appeared to be homogeneous by Davis and NaDodSO₄ polyacrylamide gel electrophoresis after albumin fraction was treated with organic cation, rivanol (2-ethoxy-6, 9, diaminoacridine lactate). The physico-chemical properties on purified albumin fraction were characterized by means of molecular weight determination, -SH content, extinction and sedimentation coefficient, etc.