Purity ~95%. Purified by HPLC. Osteonectin is an acidic, noncollagenous glycoprotein (Mr=29,000) originally isolated from fetal and adult bovine bone matrix (1-5). In vitro bovine bone osteonectin binds type I collagen, calcium (Kd=3x10(-7)M) and hydroxyapatite (Kd=8x10(-8)M) and has been shown to be a potent inhibitor of hydroxyapatite seeded crystal growth (6). In this context it has been suggested that osteonectin may play an important role in the regulation of bone metabolism by binding hydroxyapatite to collagen. Recently, proteins homologous to osteonectin nave been identified in a number of cell types, most of which are associated with extracellular matrix production (7). The amino acid sequence (from cDNA sequences) of one of these proteins, human placental SPARC, is identical to human bone osteonectin. Osteonectin has also been identified as an alpha granule component of human platelets and is secreted during platelet activation. A small portion of the secreted osteonectin is