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The purpose of this study was to determine the calcium content of human dentine under conditions of three basic assumptions which are considered to be most plausible: (1) calcified tissue is calcium-rich and noncalcified tissue is calcium-poor; (2) during the formation of calcified tissue, calcium is uniformly distributed between water and organic matrix; (3) the rate of mineral formation is constant during the formation of calcified tissue. Samples of human dentine were exposed to a solution of 3 M HCl for different periods of time, dried, and mineralized, or the HCl was removed from the tissue before the mineral was formed. The calcium content of the tissues was measured with atomic absorption spectroscopy, and the results indicate that these assumptions are not valid. For instance, mineralized tissues contain about 4.6% calcium, whereas demineralized tissues contain only 0.36%. Furthermore, the distribution of calcium between water and organic matrix appears to be dependent on the amount of calcium in the tissue. Thus, mineralized tissue contains about 5% calcium in a water-poor organic matrix, whereas demineralized tissue contains about 1% calcium in a water-rich organic matrix. Although it is not possible to separate calcium-rich components from calcium-poor components in a given tissue, the results of this study should provide a better understanding of the chemical processes occurring during the formation of human dentine.Eukaryotic proteins are targeted to the plasma membrane through a stepwise sequence of interactions with three major classes of targeting signals, the hydrophobic domain, the phosphate moiety, and the basic amino acid rich carboxy-terminal domain. These signals are comprised of several distinct motifs with very specific physical and chemical properties. The hydrophobic domain is usually the first signal encountered on a protein, usually immediately after the initiation codon. The hydrophobic domain consists of a long stretch of nonpolar amino acids and is a typical property of integral membrane proteins. A second signal usually occurs at the carboxyl terminus of a protein. It is comprised of a string of basic amino acids (usually arginines, lysines, and/or histidines) that is generally rich in the amino acid lysine. In the case of secretory proteins, these signals can be modified by a third signal, which is the phosphate moiety. This modification is also called prenylation and occurs by far the most commonly used type of signal. Prenylation is used to target the protein to the endoplasmic reticulum (ER). 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