Literature DB >> 2836344

Stabilities of lanthanide-protein complexes.

K Schomäcker1, D Mocker, R Münze, G J Beyer.   

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.

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Year:  1988        PMID: 2836344     DOI: 10.1016/0883-2889(88)90182-7

Source DB:  PubMed          Journal:  Int J Rad Appl Instrum A        ISSN: 0883-2889


  2 in total

1.  Pharmacokinetics and biodistribution of samarium-153-labelled OC125 antibody coupled to CITCDTPA in a xenograft model of ovarian cancer.

Authors:  F Kraeber-Bodéré; A Mishra; P Thédrez; A Faivre-Chauvet; M Bardiès; S Imai; J Le Boterff; J F Chatal
Journal:  Eur J Nucl Med       Date:  1996-05

2.  Distribution and excretion of lanthanides: comparison between europium salts and complexes.

Authors:  D Bingham; M Dobrota
Journal:  Biometals       Date:  1994-04       Impact factor: 2.949

  2 in total

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