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Purification of a hydrophobic surfactant peptide using high-performance liquid chromatography

✍ Scribed by Pirkko Arjomaa; Mikko Hallman

Publisher: Elsevier Science
Year: 1988
Tongue: English
Weight: 444 KB
Volume: 171
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(88)90143-1

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✦ Synopsis

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.

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