Abstract
Summary
A soluble bone morphogenetic protein (BMP) along with other noncollage-nous proteins including only a relatively insignificant quantity of hydroxyproline-con-taining peptides were extracted from rabbit cortical bone by the action of an aqueous-nonaqueous solvent mixture. As it is bound by carbohydrate recognition and hydropho-bic interaction with Con A, BMP has an essential characteristic of a glycoprotein. When α-methyl mannoside and ethylene gly-col elutes of proteins bound to a Con-A column are implanted inside of double-walled diffusion chambers, deposits of cartilage and bone develop on the outside. While estimates of the quantity of BMP are less than 0.01% of the dry weight of bone matrix, it is possible to concentrate and purify a biologically active BMP by application of the principles of hy-drophobic protein chemistry.
Get full access to this article
View all access options for this article.