Distribution and characterization of mineral-binding phosphoprotein particles in Bivalvia.

Representative species of four bivalve subclasses were examined for the presence of mineral-binding phosphoprotein particles in the physiological fluids. The particles were identified in Heterodont bivalves only, and particles from nine different Heterodont species were isolated and characterized. All phosphoprotein particles are internally cross-linked via histidinoalanine residues. In all species over 80% of the amino acid residues in the particles are aspartic acid, phosphoserine (and/or phosphothreonine), and histidine. These amino acids are probably the only residues directly related to mineral ion binding, since all phosphoprotein particles bind mineral irrespective of the minor amino acid content, which is species dependent. In their native state the phosphoprotein particles contain large amounts of calcium, magnesium, and inorganic phosphate ions (up to 45 metal ions and 8 phosphate ions per 100 amino acid residues) and trace amounts of transition elements. Evidence for the presence of calcium phosphate complexes in the native phosphoprotein particles was obtained by observing a concomitant increase in the inorganic phosphate and calcium ion content of the particles with pH in vivo.