Rapid identification of probiotic lactobacillus biosurfactant proteins by ProteinChip tandem mass spectrometry tryptic peptide sequencing.
A novel ProteinChip-interfaced tandem mass spectrometer was employed to identify collagen binding proteins from biosurfactant produced by Lactobacillus fermentum RC-14. On-chip tryptic digestion of the captured collagen binding proteins resulted in rapid sequence identification of five novel tryptic peptide sequences via collision-induced dissociation tandem mass spectrometry.
Reid
Gregor
G
Lawson Health Research Institute, St. Joseph's Health Care, 268 Grosvenor St., London, Ontario N6A 4V2, Canada.
Gan
Bing Siang
BS
She
Yi-Min
YM
Ens
Werner
W
Weinberger
Scot
S
Howard
Jeffrey C
JC
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D030562:Databases, Protein; D007778:Lactobacillus / Q000737:chemistry / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D020411:Oligonucleotide Array Sequence Analysis; D010455:Peptides / Q000737:chemistry; D019936:Probiotics; D013501:Surface-Active Agents / Q000737:chemistry*; D014357:Trypsin / Q000378:metabolism
D001426:Bacterial Proteins; D010455:Peptides; D013501:Surface-Active Agents; D003094:Collagen; D014357:Trypsin