Observations on the chemical nature of lead in human blood serum.
1. The binding of lead to human blood serum, and components of serum, was studied by titration with the addition of Pb(NO3)2 solution, monitoring the free Pb2+ concentration with a Pb2+ electrode, and by equilibrium dialysis. 2. In fresh serum, about 4999 out of 5000 parts of added lead were bound. This suggests that the free Pb2+ concentration is around 1/5000th of the total lead concentration in the serum of normal subjects, i.e. about 1 x 10(-12) mol/l. 3. About 60% of the binding of lead in serum is abolished by standing in air, by dialysis or by treatment with N-ethylmaleimide. This appears to be due to the presence of thiol compounds, mainly cysteine. The remaining 40% appears to be due to protein, mainly albumin.
Al-Modhefer
A J
AJ
Biomedical Sciences Division, King's College London.
Bradbury
M W
MW
Simons
T J
TJ
D001798:Blood Proteins / Q000378:metabolism; D006801:Humans; D007854:Lead / Q000097:blood* / Q000378:metabolism; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000378:metabolism
D001798:Blood Proteins; D013438:Sulfhydryl Compounds; D007854:Lead