Whey proteins in milk were analyzed by polyacrylamide gel electrophoresis and compared with respect to electrophoregrams, densitograms and concentrations of whey proteins in raw and market milk classified according to 3 kinds of pasteurization by low temperature long time. high temperature short time and ultra-high temperature short time. Relative composition of major whey protein constituents such as bovine serum albumin, ${alpha};-;lactalbumin;and;{eta}-lactoglobulin$ in raw milk were 3.71:11.44:84.85 and not affected by low temperature long time and high temperature short time pasteurization, even though there were the tendencies of some declining in the actual concentrations. But by ultra-high temperature short time pasteurization compositions of whey protein were changed to 0: 64.75: 35 in which reflected the disapprearance of bovine serum albumin and the extensive decrease of ${eta}-lactoglobulin$. Storage of low temperature pasteurized milk at $5^{circ}C$ resulted in a slight decrease of ${alpha};-;lactalbumin;a;{eta}-lactoglobulin$, but storage at $25^{circ}C$ did not make any changes until3rd days of storage. Most of whey proteins in high temperature short time pasteurized milk were not affected during storage at $5^{circ}C;and;25^{circ}C$, but bovine serum albumin and ${alpha};-lactalbumin$ diminished in 2-3 days of storage. Whey proteins of milk treated with ultra-high temeperature were not affected during storage at $5^{circ}C;and;25^{circ}C$ except a slight decrease of ${alpha};-lactalbumin$ in 2nd day of storage at $5^{circ}C$.