Sarcoplasmic proteins and myofibrillar proteins were extracted from Chinese sausage. Protein carbonyl,sulfydryl group contents and protein turbidity,protein degradation and solubility were measured and the effect of protein oxidation on aggregation,proteolysis and solubility during drying process was studied. The protein carbonyl content was increased and SH group number was decreased. Protein turbidity and Surface hydrophobicity( H0) increased,which was associated with the degree of protein oxidation. Proteolytic susceptibility was influenced by the degree of protein oxidation. The protein solubility determinations suggested that hydrogen bonds,hydrophobic interactions,disulphide bonds and ionic bonds are the main bonds in forming three-dimensional network structure of sausage proteins.