[HTML][HTML] Heparin-binding histidine and lysine residues of rat selenoprotein P
RJ Hondal, S Ma, RM Caprioli, KE Hill… - Journal of Biological …, 2001 - ASBMB
Selenoprotein P is a plasma protein that has oxidant defense properties. It binds to heparin
at pH 7.0, but most of it becomes unbound as the pH is raised to 8.5. This unusual heparin
binding behavior was investigated by chemical modification of the basic amino acids of the
protein. Diethylpyrocarbonate (DEPC) treatment of the protein abolished its binding to
heparin. DEPC and [14 C] DEPC modification, coupled with amino acid sequencing and
matrix-assisted laser desorption ionization-time of flight mass spectrometry of peptides …
at pH 7.0, but most of it becomes unbound as the pH is raised to 8.5. This unusual heparin
binding behavior was investigated by chemical modification of the basic amino acids of the
protein. Diethylpyrocarbonate (DEPC) treatment of the protein abolished its binding to
heparin. DEPC and [14 C] DEPC modification, coupled with amino acid sequencing and
matrix-assisted laser desorption ionization-time of flight mass spectrometry of peptides …
