Abstract
To identify the native ligands of tear lipocalins, tear proteins were separated by size exclusion chromatography and the lipid content in the major protein fractions identified. Lipids extracted from native tears and purified tear lipocalins comigrated with fatty acids, fatty alcohols, phospholipids, glycolipids, and cholesterol on thin layer chromatograms. Abundant stearic and palmitic acids as well as cholesterol, and lesser amounts of lauric acid were specifically identified in extracts of purified lipocalins by gas chromatography-mass spectroscopy. A preliminary study of the ligand-protein interaction was carried out using nitroxide spin-labeled lipids.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Carrier Proteins / chemistry
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Carrier Proteins / isolation & purification
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Carrier Proteins / metabolism*
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Chromatography, Gel
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Chromatography, Ion Exchange
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Chromatography, Thin Layer
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Electron Spin Resonance Spectroscopy
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Electrophoresis, Polyacrylamide Gel
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Eye Proteins / chemistry
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Eye Proteins / isolation & purification
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Eye Proteins / metabolism*
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Gas Chromatography-Mass Spectrometry
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Humans
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Ligands
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Lipid Metabolism*
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Lipids / isolation & purification
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Lipocalin 1
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Salivary Proteins and Peptides / chemistry
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Salivary Proteins and Peptides / isolation & purification
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Salivary Proteins and Peptides / metabolism*
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Tears / chemistry
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Tears / metabolism*
Substances
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Carrier Proteins
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Eye Proteins
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LCN1 protein, human
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Ligands
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Lipids
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Lipocalin 1
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Salivary Proteins and Peptides
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tear proteins