The isolation of non-collagen protein moiety from dentin collagen

Abstract

Purified decalcified bovine dentin matrix contains a small amount of bound phosphorous but otherwise appears to have a composition typical of mammalian collagens. Prolonged oxidative degradation of the matrix with alkaline sodium metaperlodate resulted in solubillzation of about 30% of the matrix and this portion contained more than 70% of the phosphorous and a major part of the carbohydrate residue. Fractionation of the solubillzed dentin by free flow electrophoresls, at pH 4.8, led to the isolation of a rapidly moving homogeneous anionic component (deslgned F component) and two slower moving anionic components which constituted the major percentage of this product.

DOI: 10.1007/BF02065198

Cite this paper

@article{Carmichael1968TheIO, title={The isolation of non-collagen protein moiety from dentin collagen}, author={David J. Carmichael and Eric T. Wang and Arthur Veis}, journal={Calcified Tissue Research}, year={1968}, volume={2}, pages={16-16} }