High-performance liquid chromatographic separation of peptides on a diol-Gly-Phe-Phe tripeptide-bonded phase.
The retention characteristics of some selected peptides (mol. wt. less than 2000 a.m.u.) have been investigated on a diol-Gly-Phe-Phe partitioning phase, bound to 5-microns porous silica. The hydrophobic, positively charged peptides can be separated with mild mobile phases, containing only acetonitrile and phosphate buffer. The peptide selectivity of the diol-Gly-Phe-Phe-bonded phase is uniquely different from that of a C8 column. The dependence of capacity factors on mobile phase pH, ionic strength, and organic solvent concentration demonstrated that the partitioning mechanisms of the diol-Gly-Phe-Phe phase involve multifunctional reversed-phase and cation-exchange processes.
Pinkerton
T C
TC
Control Division, Upjohn Company, Kalamazoo, MI 49001.
Koeplinger
K A
KA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D009842:Oligopeptides; D010455:Peptides / Q000032:analysis*; D011506:Proteins / Q000032:analysis; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D009842:Oligopeptides; D010455:Peptides; D011506:Proteins