title: Observations on the chemical nature of lead in human blood serum.
abstract: 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.
authors.affiliation: Biomedical Sciences Division, King's College London.
authors.forename: A J
authors.initials: AJ
authors.lastname: Al-Modhefer
authors.forename: M W
authors.initials: MW
authors.lastname: Bradbury
authors.forename: T J
authors.initials: TJ
authors.lastname: Simons
mesh_terms: D001798:Blood Proteins / Q000378:metabolism; D006801:Humans; D007854:Lead / Q000097:blood* / Q000378:metabolism; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D013438:Sulfhydryl Compounds; D007854:Lead