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pubmed-article:3407916pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:3407916pubmed:articleTitlePurification of a hydrophobic surfactant peptide using high-performance liquid chromatography.lld:pubmed
pubmed-article:3407916pubmed:affiliationChildren's Hospital, University of Helsinki, Finland.lld:pubmed
pubmed-article:3407916pubmed:publicationTypeJournal Articlelld:pubmed
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