Abstract: The velvet antler polypeptide was extracted and purified by gel filtration, ion exchange chromatography and HPLC, which showed a single peak in HPLC chromatography and a single band in SDS-PAGE. The molecular weight measured by MALDI/TOF/MS spectrum is 3 095.1. The polypeptide consists mostly of Ala, Phe, Lys, Gly, but no Cys. The N-terminal amino acid of the polypeptide was detected by FDNB method to be Val. The experiment of pharmaceutical activity indicated that the polypeptide could obviously stimulate proliferation of the epithelial cells and BRL cells.

Key words: velvet antler, polypeptide, purify, pharmaceutical activity