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Pulmonary surfactant protein SP‐B is significantly more immunoreactive in anionic than in zwitterionic bilayers
Author(s) -
Marı́a Oviedo Jose,
Casals Cristina,
Pérez-Gil Jesús
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02350-x
Subject(s) - phosphatidylethanolamine , phosphatidylcholine , phosphatidylserine , phosphatidic acid , cardiolipin , phosphatidylglycerol , chemistry , phospholipid , polyclonal antibodies , pulmonary surfactant , biochemistry , phosphatidylinositol , micelle , chromatography , antibody , membrane , biology , organic chemistry , kinase , aqueous solution , immunology
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.