title: Stabilities of lanthanide-protein complexes.
abstract: After incubation of both serum and HSA solutions with radioactive lanthanide complexes the binding constants of the corresponding lanthanide-protein complexes formed in the protein solutions under physiologic conditions, pH: 7.4, temperature: 310 K, isotonic ionic strength: 0.15 mol/L, were determined. The association constants of the lanthanide-protein complexes formed both in serum and HSA-solutions are equal within the experimental error. In conclusion, serum albumin binding predominates for the radiolanthanides. With the decrease of the ionic radii from 1.034 A (Ce) to 0.858 (Yb) the association constants increased by five orders of magnitude from 1 g Kpr = 4.90 (Ce) to 1 g Kpr = 9.54 (Yb). Further, a serum fractionation with alcohol was carried out to prove that the albumin fraction of serum is responsible for the lanthanide binding in blood.
authors.affiliation: Central Institute of Nuclear Research, Dresden, G.D.R.
authors.forename: K
authors.initials: K
authors.lastname: Schomäcker
authors.forename: D
authors.initials: D
authors.lastname: Mocker
authors.forename: R
authors.initials: R
authors.lastname: Münze
authors.forename: G J
authors.initials: GJ
authors.lastname: Beyer
mesh_terms: D001798:Blood Proteins; D004355:Drug Stability; D006801:Humans; D008674:Metals, Rare Earth; D011485:Protein Binding; D012709:Serum Albumin
chemical_list: D001798:Blood Proteins; D008674:Metals, Rare Earth; D012709:Serum Albumin