Dissociative extraction and partial purification of osteogenin, a bone inductive protein, from rat tooth matrix by heparin affinity chromatography

R. W. Katz, A Hari Reddi

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Implantation of demineralized tooth matrix in subcutaneous sites results in new bone formation locally. The osteoinductive activity of the tooth matrix was dissociatively extracted in 4.0 M guanidine hydrochloride and the residue was devoid of biologic activity. The bone inductive protein, osteogenin, was partially purified by heparin affinity chromatography. The heparin binding fraction initiated the bone differentiation cascade when implanted with guanidine extracted, inactive bone or tooth matrices. These results imply a cooperative interaction between the soluble osteogenin and collagenous substratum in bone induction.

Original languageEnglish (US)
Pages (from-to)1253-1257
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume157
Issue number3
DOIs
StatePublished - Dec 30 1988
Externally publishedYes

Fingerprint

Bone Morphogenetic Protein 3
Affinity chromatography
Affinity Chromatography
Purification
Heparin
Rats
Tooth
Bone
Bone and Bones
Guanidine
Proteins
Osteogenesis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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AB - Implantation of demineralized tooth matrix in subcutaneous sites results in new bone formation locally. The osteoinductive activity of the tooth matrix was dissociatively extracted in 4.0 M guanidine hydrochloride and the residue was devoid of biologic activity. The bone inductive protein, osteogenin, was partially purified by heparin affinity chromatography. The heparin binding fraction initiated the bone differentiation cascade when implanted with guanidine extracted, inactive bone or tooth matrices. These results imply a cooperative interaction between the soluble osteogenin and collagenous substratum in bone induction.

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