The crosslink ability with HCH0 of different components （sub-units） in collagen and gelatin were investigated. We made a series of comparisons between the components. The difference of crosslink ability was discussed. There is no obvious difference between the crosslink ability of α βcomponents in acid soluble collagen and those of the same components in photographic gelatin. The crosslink ability of α2 is greater than that of α1: but the crosslink ability of β11 is similar to that of β12, and β components have obviously hydroIyzed during crosslink process. This situation happens in components of collagen as well as in components of gelatin.
