Abstract: A systematic research was made to observe and compare the hydrolysis capacity of different individual conformational components (α₁, α₂, β₁₁, β₁₂)seperated from acid-soluble collagen. The experimental data clearly showed that under the liquid solution(pH=7.0), after hydrolysis for 4.5 h, α₁, α₂, β₁₁, β₁₂ had all greatly hydrolyzed, and the hydrolysis capacity of α₁ matched that of α₂, the hydrolysis capacity of β₁₁ was as great as that of β₁₂; but under the salt solution, the hydrolysis capacity of α₁ was greater than that of α₂, the hydrolysis capacity of β₁₁ was greater than that of β₁₂. The difference of hydrolysis capacity between α₁ and α₂, under salt condition was likely due to the content difference of Glu & Asp which could complex with Au³⁺ in the α components. The main results and conclusions might be of reference value in deeply exploiting the research of collagen reactivity and in practically solving the problem how to maintain and improve the physico mechanical properties of gelatin emulsion layer or a gelatin coating layer in general.

Key words: acid-soluble collagen, hydvolysis, polg acrylamied gel electrophoresis