The findings suggest that there was no significant difference in the tag quality between the conventional technique (Control) and the 'bleach-etch-seal' technique (Treatment 1). There was no benefit in pre-treating with NaOCl alone (without etch) before sealing. This research also showed that there was a high-predicted probability of obtaining 'poor' sealant tags in MIH enamel, regardless of which of the three treatments was used.

Calcium-and hydroxyapatitebinding properties of glucuronic acid-rich and iduronic acid-rich glycosaminoglycans and proteoglycansEmhery G. R ees S. Hall R , Rose K, WaddingTon R. She/lis P: Calcium-and hydroxyapatite-binding properties of glucuronic acid-rich all(l iduronic acid-rich glycosaminog/_I'C (/11.\' and proteoglycans. Eur J Oral Sci 1998; 106 ( suppl I ): 267 273. g Eur J Oral Sci. 1998 This study describes the interaction of a small chondroitin sulphate proteoglycan and the glycosaminoglycans chondroitin 4-su lphate, dcrmatan sulphate and heparan sulphate with hydroxyapatite. All macromolecu les possessed a high affinity, with the iduronic acid-rich dermatan sulphate and heparan sulphate displaying higher adsorption maxima than the glucuronic acid-rich chondroitin 4-sulphate. At similar concentrations, dermatan sulphate produced a 30'X, inhibition of hydroxyapatite-induced crystal growth, whilst chondroitin 4-sulphate yielded 50'Y., inhibition. Estimation of the calcium binding capacity of these glycosaminoglycans using equilibrium dialy i indicated that chondroitin 4-sulphate bound five times more calcium than • rmatan sulphate at a calcium concentration similar to that of serum . The data indicate a possible important role for chondroitin 4-sulphate in dentinogenesis where it is the dominant glycosaminoglycan, since it could act as a capture point for calcium ions during mineralisation , with the leucine-rich domain of its parent proteoglycan acting as anchor points to type 1 collagen.