title: Purification of a hydrophobic surfactant peptide using high-performance liquid chromatography.
abstract: A 4- to 6-kDa hydrophobic peptide (SP4-6) was purified from human pulmonary surfactant. Sep Pak Florisil cartridges removed most of the lipids and the 18-kDa peptide. Analytical wide-pore reversed-phase HPLC column separated a single peptide that contained no detectable lipids (less than 1 nmol/2.5 micrograms protein). N-terminal analysis indicated that this peptide was pure, but the N-terminal amino acid was blocked. The peptide was capable of restoring the in vitro surface properties of synthetic phospholipids, which is characteristic of native lung surfactant.
authors.affiliation: Children's Hospital, University of Helsinki, Finland.
authors.forename: P
authors.initials: P
authors.lastname: Arjomaa
authors.forename: M
authors.initials: M
authors.lastname: Hallman
mesh_terms: D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008055:Lipids / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification* / Q000502:physiology; D011506:Proteins / Q000302:isolation & purification; D011663:Pulmonary Surfactants / Q000032:analysis*
chemical_list: D008055:Lipids; D010455:Peptides; D011506:Proteins; D011663:Pulmonary Surfactants