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J. Biol. Chem., Vol. 263, Issue 31, 15938-15945, Nov, 1988

Isolation of new phosphorylated glycoprotein from mineralized phase of bone that exhibits limited homology to adhesive protein osteopontin

JP Gorski and K Shimizu
Division of Molecular Biology and Biochemistry, School of Basic Life Sciences, University of Missouri-Kansas City 64110.

Extracts of the mineralized phase of rat calvaria were shown to contain bone acidic glycoprotein-75, a new phosphorylated glycoprotein which co- purifies with small bone proteoglycans through anion-exchange chromatography. Final purification of each was brought about with a subsequent hydroxyapatite step. Bone acidic glycoprotein-75 is 75,000 in molecular weight with a 29.3% molar content of acidic amino acid residues, a 7.0% (w/w) content of sialic acid, and a 7.9% molar content of organic phosphate. Its N-terminal sequence was determined as Leu-Pro- Val-Ala-Arg-Tyr-Gln-Asn-Thr-Glu-Glu-Glu-Glu-. Because the size and charge density properties of bone acidic glycoprotein-75 are similar to those reported for rat bone sialoprotein II, calvarial sialoprotein II was also purified to homogeneity, and its amino acid composition and N- terminal sequence were determined. The sequence results showed an identity with the first 5 residues of human sialoprotein II and a complete lack of homology with bone acidic glycoprotein-75, which, furthermore, did not bind anti-sialoprotein II antibodies. Although the N-terminal sequence of bone acidic glycoprotein-75 appears to be unique, a 33% homology is shared with rat adhesive protein osteopontin. Affinity-purified antibodies against osteopontin were found to specifically bind to bone acidic glycoprotein-75 and to sialoprotein II upon immunoblotting, whether as purified proteins or as components of crude calvarial extracts. In summary, bone acidic glycoprotein-75 is a new phosphorylated glycoprotein from the mineralized compartment of rat calvarial tissue with a limited structural homology to osteopontin.
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