Analysis of tryptic digests of bovine beta-casein by reversed-phase high-performance liquid chromatography.
Reversed-phase high-performance liquid chromatography (RP-HPLC) was used to separate the tryptic peptides of beta-casein. A gradient of 0-50% acetonitrile in 0.1% trifluoroacetic acid at a flow-rate of 0.8 ml/min resolved ten of the thirteen peptides. A modified gradient resolved the three peptides eluted at ca. 25% acetonitrile. RP-HPLC proved superior to high-voltage paper electrophoresis in analysis time, resolution and flexibility. The methods developed for the analysis of proteolysis of the milk protein, beta-casein, are now being applied to study the action of extracellular proteases from dairy bacteria on milk proteins.
Leadbeater
L
L
Department of Microbiology, Edinburgh School of Agriculture, U.K.
Ward
F B
FB
D000818:Animals; D002364:Caseins / Q000302:isolation & purification*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003619:Dansyl Compounds; D004590:Electrophoresis, Paper; D006868:Hydrolysis; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin
D002364:Caseins; D003619:Dansyl Compounds; D010446:Peptide Fragments; D014357:Trypsin