Phospholipase A2 complexes with gadolinium (III) and interaction of the enzyme-metal ion complex with monomeric and micellar alkylphosphorylcholines. Water proton nuclear magnetic relaxation studies.

@article{Hershberg1976PhospholipaseAC,
  title={Phospholipase A2 complexes with gadolinium (III) and interaction of the enzyme-metal ion complex with monomeric and micellar alkylphosphorylcholines. Water proton nuclear magnetic relaxation studies.},
  author={Robert D. Hershberg and George H Reed and A. J. Slotboom and G H deHaas},
  journal={Biochemistry},
  year={1976},
  volume={15 11},
  pages={2268-74}
}
Gadolinium (III) binds competitively with calcium(II) to porcine pancreatic phospholipase A2 (EC 3.1.1.4) and its zymogen. The enzyme-Gd3+ complex exhibits 4% of the hydrolytic activity of the corresponding Ca2+ complex toward a dispersion of dioctanoyllecithin. Dissociation constants for the Gd3+ complex of enzyme and proenzyme were evaluated from water… CONTINUE READING