Abstract
Binding of polyclonal and monoclonal antibodies, quantitated by enzyme-linked immunosorbent assay, to porcine SP-B reconstituted in different phospholipid bilayers has been used to assess differences in protein structure due to lipid–protein interactions. SP-B bound significantly more antibodies when it was reconstituted in bilayers made of anionic phospholipids (phosphatidic acid, cardiolipin, phosphatidylglycerol, phosphatidylinositol or phosphatidylserine) than in zwitterionic bilayers (phosphatidylcholine, phosphatidylcholine/cholesterol, or phosphatidylethanolamine) or in fatty acid micelles (made of salts of palmitic or stearic acids). These differences in immunoreactivity can be important in the development of quantitation methods for SP-B in clinical samples based on immunological techniques.
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