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Purification of a skeletal growth factor from human bone

, : Purification of a skeletal growth factor from human bone. Biochemistry 21(14): 3502-3507

A skeletal growth factor was isolated and purified from demineralized human bone matrix. A dose of 6 .mu.g/ml of the purified factor significantly increased the proliferation rate of embryonic chick bone cells in serum-free culture (292% of controls, P < 0.0001) but had no effect on embryonic chick skin cells plated at the same initial density. The factor is sensitive to inactivation by trypsin and urea, but not by collagenase, 20% butanol, or 1% mercaptoethanol. It is also resistant to inactivation by heat (stable for 15 min a C) and extremes of pH (stable for 30 min at C from pH 2.5 to 10.0). Purification of the active factor by selective heat and acid precipitations, molecular sieve column chromatography, and preparative polyacrylamide gel electrophoresis provided a material that was homogeneous by the criteria of high pressure liquid chromatography, polyacrylamide gel electrophoresis, and isoelectric focusing. The apparent MW is 83,000. The purified factor increases bone cell proliferation at doses comparable to other mitogens: 0.3 .mu.g/ml (3.6 nM) significantly increases DNA synthesis to 231% of controls (P < 0.001). The purified factor was also active on cultured embryonic chick bones, enhancing the growth rate of tibiae and femurs, as measured by increased dry weight (185% of controls, P < 0.025) and [3H]proline incorporation (164% of control, P < 0.001), respectively.


PMID: 6288076

DOI: 10.1021/bi00257a037

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