he aim of this study was to introduce a simple, reproducible, and less expensive method for isolation of ?-lactalbumin from cow’s milk while retaining their antigenicity. Whey (lactoserum) was obtained by isolating casein from defatted milk using hydrochloric acid. Globulins were then precipitated from whey by half-saturated ammonium sulfate. The proteins in the supernatant were also fractionated using diethylaminoethyl cellulose chromatography in which ?-lactoglobulin was separated from ?-lactalbumin and bovine serum albumin. The latter two proteins that co-eluted in anion-exchange chromatography were then gently isolated from each other by Sephadex G-50 gel filtration. Pure ?-lactoglobulin was also obtained by anion-exchange chromatography of the ammonium sulfate-precipitated globulins. Our results showed high purity and well-preserved antigenicity of ?-lactalbumin, ?-lactoglobulin, and bovine serum albumin thus purified.
The experiment was carried out successful and the The protein concentration was determined and was determined Our results showed high purity and well-preserved antigenicity of ?-lactalbumin