Abstract

Laser Raman spectra of ox tibia and of reconstituted rat tail tendon have been obtained and have been compared with the infrared spectra of calcified tissue and collagen. The most intense Raman bands in the calcified tissue originate from the symmetric phosphate modes; however, several of the backbone and side chain modes of collagen are also apparent. There is some evidence that both proline and phenylalamine in the collagen contribute to the spectrum. The Raman spectrum of reconstituted, collagen was difficult to separate from the fluorescence background. Only six distinct bands could be obtained, divided between peptide and sidechain modes. Differences between reconstituted and calcified collagen spectra may originate from partial denaturation of the former in the laser beam. Other differences seem to be genuine chemical manifestations.

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