Identification of an essential lysine residue in the phosphatidylcholine-transfer protein from bovine liver by modification with phenylisothiocyanate.
Modification by phenylisothiocyanate inhibits the phosphatidylcholine-transfer protein from bovine liver. Inhibition by this apolar reagent was greatly enhanced in the presence of vesicles, indicating that an effective modification of an essential lysine residue(s) from the interface may occur. Labeling with [14C]phenylisothiocyanate demonstrated that Lys55 was the major site of modification. We propose that Lys55 is part of the peptide segment that interacts with the membrane.
D000727:Androgen-Binding Protein; D000818:Animals; D002352:Carrier Proteins / Q000032:analysis*; D002417:Cattle; D003488:Cyanogen Bromide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D017879:Isothiocyanates; D008099:Liver / Q000032:analysis*; D008239:Lysine / Q000032:analysis*; D049294:Phospholipid Transfer Proteins; D013861:Thiocyanates / Q000494:pharmacology*
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D017879:Isothiocyanates; D049294:Phospholipid Transfer Proteins; D013861:Thiocyanates; C005441:phenylisothiocyanate; D008239:Lysine; D003488:Cyanogen Bromide