Abstract
Summary
The ability of protamine, lysozyme, and bovine serum albumin to compete for calcium binding sites on acidic phospholipids provides a method for quantitative studies of the electrostatic interactions of proteins with phospholipids. The results demonstrate the reversible, stoichiometric binding of proteins with phospholipids. Crude cephalin binds arginine but not glycine, leucine, or phenylalanine. The data suggest a strong electrostatic interaction between negatively charged phospholipids and positively charged proteins and indicate that electrostatic bonding may occur in lipoproteins.
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