Camel (Camelus dromedarius) milk caseins and whey proteins compared to bovine milk proteins and its relation to different heat treatments were detected using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Camel milk whey proteins such as serum albumin (SA) and alpha-lactalbumin (a-La) appear to possess molecular weights similar to the respective bovine whey proteins. In camel milk, no protein bands homologous to bovine neither beta-lactoglobulin (b-Lg) nor k-casein could clearly be detected in the electrophoretic pattern and consists of large amount of serum albumin, compared to bovine whey. Camel milk whey protein showed higher heat stability than those of cow's milk. After an initial higher denaturation of whey proteins in camel milk at 65°C/30 min, which represents the conditions of conventional pasteurization caused no visible change (denaturation) in whey proteins, whilst higher heat treatment at 80 and 100°C for 30 min which is more excessive than pasteurization, resulted visible changes of the whey proteins. The present study demonstrates  the most predominated values of free amino acids (FAA) glutamic, aspartic, isoleucine and alanine respectively in both of heated caseins and whey separated from camel's milk. The FAA concentrations of camel's milk caseins appear to be more heat stable than those of camel's milk whey, which has high loss percentages in FAA than of caseins