ISOLATION OF HEN EGG-WHITE LYSOZYME, OVOTRANSFERRIN AND OVALBUMIN, USING A QUATERNARY AMMONIUM BOUND TO A HIGHLY CROSS-LINKED AGAROSE MATRIX

A single-step anion-exchange chromatographic separation of egg white p roteins was carried out using a Q Sepharose Fast Flow column. The sepa ration resulted in the isolation of two lysozyme peaks with purities o f ca. 99 and 88%, one peak of ovotransferrin purified to ca. 75% and t wo ovalbumin peaks with purities of ca. 54 and 98%. Recoveries were es timated to be ca. 60, 100 and 83% for lysozyme, ovotransferrin and ova lbumin, respectively. The amino acid compositions of all collected pea ks have also been determined. This confirmed the identity of some of t he proteins contained in these peaks.