Abstract
Bone proteins in mandibular alveolar bone from young adult rabbits (3-month-old) were extracted with 4 M guanidine hydrochloride (GuHCl), followed by 0.5M ethylenediaminetetraacetic acid (EDTA). The proteins in the EDTA extract were fractionated on Sepharose CL-6B in the presence of 4 M GuHCl, followed by HPLC using hydroxyapatite and then ‘Mono Q’ resin in the presence of 7 M urea, and a 28 kDa protein was isolated. The purified 28-kDa protein showed intense staining with silver following SDS-PAGE separation under reducing conditions. When the protein was digested with bacterial collagenase, a 19-kDa fragment was produced. However, the protein was not susceptible to cyanogen bromide. On SDS-PAGE under non-reducing conditions, the protein migrated as two bands; a new band at about 85-kDa, and the original 28-kDa band. The amino acid composition of the protein was similar to that of α1-pN-propeptide of type I procollagen from other tissues. Moreover, the characteristics of the purified 28-kDa protein were similar to those of a 28-kDa protein synthesized by rabbit alveolar bone-derived cellsin vitro.
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Maeno, M., Suzuki, N., Ohmori, Y. et al. Characterization of a 28-kDa collagenous protein extracted with EDTA from adult rabbit alveolar bone. J Bone Miner Metab 10, 18–25 (1992). https://doi.org/10.1007/BF02383457
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DOI: https://doi.org/10.1007/BF02383457