Modification of arginine residues in porcine pancreatic phospholipase A2.

@article{Fleer1981ModificationOA,
  title={Modification of arginine residues in porcine pancreatic phospholipase A2.},
  author={Edward A. M. Fleer and Wouter C. Puijk and A. J. Slotboom and Gerard De Haas},
  journal={European journal of biochemistry},
  year={1981},
  volume={116 2},
  pages={277-84}
}
Although phenylglyoxal monohydrate reacts with Arg-6 in porcine pancreatic phospholipase A2, concomittantly the alpha-amino group of the N-terminal Ala-1 residue is quantitatively transaminated. Due to this latter reaction the enzymatic activity toward micellar substrate is lost irrespective of the Arg-6 modification. Upon reaction of [7-(14)C]phenylglyoxal monohydrate with alpha-amino-blocked phospholipase A2 analogs, two molecules of the reagent were incorporated per protein molecule, which… CONTINUE READING