title: Characterization of the complex between bovine osteocalcin and type I collagen.
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.
authors.affiliation: Chemistry Department, Trinity College, Hartford, Connecticut 06106, USA. rprig@trincoll.edu
authors.forename: R V
authors.initials: RV
authors.lastname: Prigodich
authors.forename: M R
authors.initials: MR
authors.lastname: Vesely
mesh_terms: D000818:Animals; D002021:Buffers; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D015675:Osteocalcin / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects
chemical_list: D002021:Buffers; D010710:Phosphates; D015675:Osteocalcin; D003094:Collagen; D002118:Calcium