Isolation and Purification of 18KD Protein of Sika Deer Antler Plate and its Antibacterial Activity
Isolation and Purification of 18KD Protein of Sika Deer Antler Plate and its Antibacterial Activity
Lin Qi, Lu Li, Danyang Chen, Mingxiao Liu, Yan Wu and Wei Hu*
SDS-PAGE electrophoresis results of total peptides from antler plate The protein of antler plate was mainly concentrated below 29.0kDa, and a band around 20.1kDa was obvious.
The result of analytical reverse high performance liquid chromatography. A total of 15 peaks were collected. The large peak between 3.2 and 4.0 min is the solvent peak, and the peak appearing at 28.93 min has a relatively high abundance.
Molecular mass detection of the monomeric peptide. Mass of the monomeric peptide was determined by Bruker micOTOF OllQ TOF with an experimental accuracy of ± 0.1%, the peak is due to solvent interference. The molecular mass of this novel polypeptide was 18907Da.
Liquid enrichment of reversed phase high performance liquid Chromatography. The arrow in the figure showed the enriched target protein with a molecular weight of 18907Da.
Purity identification of the monomeric peptide from antler plate. Purity identification of the monomeric peptide by utilizing the HPLC, the purity of this novel polypeptide was 90%.
