Abstract:

In order to study the isolation and purification of an active peptide component from velvet antler of sika deer(Cervus nippon Temminck), confirm the primary structure of the novel peptide and compare the sequence and the activity with those of velvet antler of red deer(Cervus elaphus Linaeus), the velvet antler polypeptide was isolated and purified by ion exchange chromatography, gel filtration and RP-HPLC, which showed a single peak in HPLC chromatography and a single band in SDS-PAGE. The molecular weight was measured by MALDI-TOF MS. This polypeptide consists of a single linear chain of 32 amino acid residues VLSATDKTNVLAAWGKVGGNAPAFGAEALERM. The experiment results of bioactivity showed that the polypeptide had stimulant effects on the growth of rat epithelial cells, rabbit costal chondrocytes and rat NIH3T3 cell line, respectively in vitro. The straight chain of 32 amino acid residues of the velvet antler polypeptides of Cervus nippon Temminck was consisted with that of Cervus elaphus Linaeus, but they make a difference of 5, 8, 11 and 30 amino acid. There was no effect on stimulating proliferation of cells.

Key words: Velvet antler of Cervus nippon Temminck, Polypeptide, Promoted proliferation of cell