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Characterization of the complex between bovine osteocalcin and type I collagen.

作者信息

Prigodich R V, Vesely M R

机构信息

Chemistry Department, Trinity College, Hartford, Connecticut 06106, USA.

出版信息

Arch Biochem Biophys. 1997 Sep 15;345(2):339-41. doi: 10.1006/abbi.1997.0254.

Abstract

This study examined the association of bovine osteocalcin with type I collagen under a variety of conditions, including different buffers, pH, and concentrations of phosphate and Ca(II). The data showed that osteocalcin binds to type I collagen reversibly with a binding constant which varies from 4000 to 160,000 M(-1), depending upon the exact conditions. Furthermore, the results indicated that there is only one osteocalcin binding site per collagen molecule. The absence or presence of Ca(II) and/or phosphate in the buffer had little effect on complex formation.

摘要

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