The Degradation of Human Dentine Collagen by Trypsin

Insoluble collagen was prepared from the roots of human teeth and chemically characterized. This material was found susceptible to digestion with trypsin, at both 20°C and 37°C, yielding small dialysable peptides. Insoluble bovine tendon collagen was not digested to any significant extent under the experimental conditions employed. The susceptibility of the human dentine collagen could not be correlated with peculiarities of chemical composition nor with various treatments employed during its preparation. Re-equilibration of the dentine collagen with calcium ions did not result in any stabilization towards trypsinization. The origin of this susceptibility is discussed in relation to the organization and life-history of human root dentine.