Abstract：Bovine bone collagen was hydrolyzed by neutral protease, and then the hydrolyate was separated and purified
using ultrafiltration and gel chromatography. The antibacterial peptides obtained were analyzed by reverse high-performance
liquid chromatography (RP-HPLC) and matrix-assisted laser desorption/ionization cascade time of flight mass spectrometry
(MALDI-TOF-TOF-MS). The results showed that the ultrafiltration fractions with molecular weight less than 10 kD had
strong antibacterial activity against Escherichia coli. The peaks I and IV isolated by Sephadex G-25 gel chromatography had
strong antibacterial activity. By RP-HPLC and MALDI-TOF-TOF-MS analysis, the peak I contained a variety of peptides
with molecular weight between 850 and 1550 D, whereas the peak IV contained fewer peptides between 700 and 900 D.
2013, Vol. 27 
