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

作者: J P Gorski , K Shimizu

DOI: 10.1016/S0021-9258(18)37539-2

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

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