| Autor: |
Carmichael, David J., Dodd, Carole M., Nawrot, Charles F. |
| Zdroj: |
Calcified Tissue International; December 1974, Vol. 14 Issue: 1 p177-194, 18p |
| Abstrakt: |
The collagen in bone and soft tissues of lathyritic animals is known to be more soluble than that of normal animals when traditional methods of extraction are employed. To ascertain whether a similar phenomenon occures in lathyritic dentine collagen, the solubility of dentine matrix collagen was investigated in two solvents. Young adult male rats were maintained on a lathyrogenic diet for 50 days, during which time the major part of the dentine matrix collagen of the incisors was shown to have turned over completely. Decalcified dentine matrix collagen was prepared by exhaustively dialysing cleaned incisors against 0.5M acetic acid, and the non-dialysable matrix was further extracted with the same solvent, and then with 5 M guanidine hydrochloride. The dentine matrix collagen of both normal and lathyritic animals proved to be insoluble in 0.5M acetic acid; guanidine hydrochloride extraction solubilized approximately 20% of the lathyritic matrix collagen as well as a quantity of non-collagen protein, in contrast to the soft tissue and bone collagens of lathyritic animals in which greater amounts of collagen may be solubilized by this procedure. Fractionation of the guanidine hydrochloride extract from the lathyritic animals by carboxymethyl cellulose chromatography revealed an unexpectedly high ratio of α1 to α2 components considerably greater than the 2∶1 ratio demonstrated for lathyritic rat bone. These data provide evidence for significant differences between bone and dentine collagens. |
| Databáze: |
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