000166003 001__ 166003 000166003 005__ 20260204133827.0 000166003 0247_ $$2doi$$a10.1016/j.bbagen.2011.10.006 000166003 0248_ $$2sideral$$a76272 000166003 037__ $$aART-2012-76272 000166003 041__ $$aeng 000166003 100__ $$aWhite, K. N. 000166003 245__ $$aThe transfer of iron between ceruloplasmin and transferrins 000166003 260__ $$c2012 000166003 5060_ $$aAccess copy available to the general public$$fUnrestricted 000166003 5203_ $$aBackground It is over 60 years since the discovery and isolation of the serum ferroxidase ceruloplasmin. In that time much basic information about the protein has been elucidated including its catalytic and kinetic properties as an enzyme, expression, sequence and structure. The importance of its biological role is indicated in genetic diseases such as aceruloplasminemia where its function is lost through mutation. Despite this wealth of data, fundamental questions about its action remain unanswered and in this article we address the question of how ferric iron produced by the ferroxidase activity of ceruloplasmin could be taken up by transferrins or lactoferrins. Methods Overlapping peptide libraries for human ceruloplasmin have been probed with a number of different lactoferrins to identify putative lactoferrin-binding regions on human ceruloplasmin. Docking software, 3D-Garden, has been used to model the binding of human lactoferrin to human ceruloplasmin. Results Upon probing the human ceruloplasmin library with human lactoferrin, three predominantly acidic lactoferrin-binding peptides, located in domains 2, 5 and 6 of human ceruloplasmin, were identified. The docking software identified a complex such that the N-lobe of human apo-lactoferrin interacts with the catalytic ferroxidase centre on human ceruloplasmin. 000166003 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.es 000166003 590__ $$a3.848$$b2012 000166003 591__ $$aBIOPHYSICS$$b15 / 71 = 0.211$$c2012$$dQ1$$eT1 000166003 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b89 / 288 = 0.309$$c2012$$dQ2$$eT1 000166003 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion 000166003 700__ $$0(orcid)0000-0003-0862-9893$$aConesa, C. 000166003 700__ $$aS·nchez, L. 000166003 700__ $$aAmini, M. 000166003 700__ $$aFarnaud, S. 000166003 700__ $$aLorvoralak, C. 000166003 700__ $$aEvans, R. W. 000166003 773__ $$g1820, 3 (2012), 411-416$$pBiochim. biophys. acta (G)$$tBiochimica et Biophysica Acta - General Subjects$$x0304-4165 000166003 8564_ $$s723963$$uhttps://zaguan.unizar.es/record/166003/files/texto_completo.pdf$$yPostprint 000166003 8564_ $$s655527$$uhttps://zaguan.unizar.es/record/166003/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint 000166003 909CO $$ooai:zaguan.unizar.es:166003$$particulos$$pdriver 000166003 951__ $$a2026-02-04-13:18:10 000166003 980__ $$aARTICLE