抄録
Human milk lysozyme was purified successively by the ion exchange chromatography on carboxymethylcellulose and the gel filtration through Sephadex G-50. The enzyme was shown to be homogeneous with respect to ultracentrifugal, electrophoretic, and spectrophotometric patterns. In agreement with the previous finding, it was found that human milk lysozyme was similar to egg white lysozyme in the optical pH and molecular weight, although these enzymes differed in amino acid composition each other. In this paper, we attempted to establish a rapid and simple preparation method for human milk lysozyme, and found that the electrophoretic mobility of both human milk and egg white lysozymes were also different each other.
