Abstract
The infra-red spectra of 1) the decalcified films of sections, 2) thin sections cut by microtome, 3) denatured proteins of molar tooth dentin of Elephas maximus and Elephas naumanni have been examined. The results are as follows: 1) The obtained absorption bands represent protein spectra and these bands resemble those of collagen or gelatin. 2) Amide A absorption band at 3320 cm-1 in the decalcified films of E. naumanni shows higher wave number than that of so-called conchiolin at 3200〜3300 cm-1, which indicates close value to that at 3330 cm-1 of rat tail tendon collagen. 3) From the wave number of Amide I, II absorption bands of the decalcified films in the molar tooth dentin of E. naumanni, it is estimated that helical conformation which is different from α-helix and antiparallel-β-conformation exsist in these films. And the same conformation is recognized in the films of E. maximus. 4) Antiparallel-β-conformation is observed in the conchiolin fims (for example, nacreous structure, inner layer, Pinctada maxima}, this conformation may be the fundamental conformation of proteins constituting the calcifying hard tissues.
