Solubilized and insolubilized bone morphogenetic protein. | Zendy

Marshall R. Urist | Zendy; Andrzej Mikulski | Zendy; Arthur Lietze | Zendy

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Solubilized and insolubilized bone morphogenetic protein.

Author(s) -

Marshall R. Urist,

Andrzej Mikulski,

Arthur Lietze

Publication year - 1979

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.76.4.1828

Subject(s) - chemistry , ethylene glycol , chromatography , bone morphogenetic protein , concanavalin a , salt (chemistry) , glycoprotein , elution , biochemistry , bone morphogenetic protein 2 , collagenase , enzyme , organic chemistry , in vitro , gene

A bone morphogenetic protein (BMP) obtained in solution by digestion of demineralized rabbit cortical bone matrix with bacterial collagenase retains its biologically active conformation in a neutral salt/ethylene glycol mixture. BMP may be insolubilized by coprecipitation with calcium phosphate and resolubilized by chemical extraction with a neutral salt in the same solvent mixture. Upon concanavalin A-Sepharose chromatography, BMP is bound by hydrophobic interaction and carbohydrate recognition and is recovered by elution with either alpha-methyl mannoside or ethylene glycol solvent mixture. Implants of both eluates and the extracts of the coprecipitate in double-walled diffusion chambers induce transmembrane bone morphogenesis. BMP is not species specific; rabbit BMP induces new bone formation in the rat. The present observations indicate that BMP is a glycoprotein.

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