This study was based on the 462 milk samples collected from approximately 2000 cows registered in Dairy Herd Analysis Service (DHAS). Milk samples from fresh milks were phenotyped by gel electrophoresis. Milk samples were selected according to the nine possibilities of phenotype combination of $ kappa$-casein AA, AB, BB and $ beta$-lactoglobulin AA, AB and BB. Selected milk samples from fresh milks were heated at 25$ sp circ$C, 60$ sp circ$C, 70$ sp circ$C, 80$ sp circ$C and 90$ sp circ$C, respectively. Whole casein and whey protein were separated by adjusting the pH to 4.6. Quantitative determination of milk protein were performed by reverse-phase HPLC. Whole casein was separated to $ kappa$-casein ($ kappa$-Cn), $ beta$-casein ($ beta$-Cn) and $ rm alpha sb{s}$-casein ($ rm alpha sb{s}$-Cn). Whey protein was separated as immunoglobulin (Ig), bovine serum albumin (BSA), $ alpha$-lactalbumin ($ alpha$-La) and $ beta$-lactoglobulin ($ beta$-Lg). Individual milk protein fraction was quantitatively determined by relative peak area and their ratios to whey protein or casein. The denaturation of individual milk protein at different heating temperature was investigated. (Abstract shortened by UMI.)

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