Modification of the phosphatidylcholine-transfer protein from bovine liver with butanedione and phenylglyoxal. Evidence for one essential arginine residue.

1. Modification of arginine residues with 2,3-butanedione and phenylglyoxal completely inhibits the transfer activity of the phosphatidylcholine transfer protein from bovine liver. Removal of borate and butanedione leads to a slow reactivation of the protein. 2. Both alpha-dicarbonyl reagents modify three of the ten arginine residues present per protein molecule. The extent of modification is linearly related to the loss of activity. 3. Inactivation with butanedione is greatly diminished when the protein is bound to strongly negatively charged vesicles. Under these conditions a rapid modification of two arginine residues is observed. This suggests that the transfer protein contains one arginine residue essential for activity, probably as a binding site for the negatively charged phosphate group of the phosphatidylcholine molecule. 4. This study provides convincing evidence that arginine residues may play an essential role in phospholipidprotein interactions.