<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Batalha, Iris L</style></author><author><style face="normal" font="default" size="100%">Hussain, Abid</style></author><author><style face="normal" font="default" size="100%">Roque, A. C. A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Gum Arabic coated magnetic nanoparticles with affinity ligands specific for antibodies</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Molecular Recognition</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adsorption</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibodies</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibody Affinity</style></keyword><keyword><style  face="normal" font="default" size="100%">Ferric Compounds</style></keyword><keyword><style  face="normal" font="default" size="100%">Fourier Transform Infrared</style></keyword><keyword><style  face="normal" font="default" size="100%">gum arabic</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">Magnetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Metal Nanoparticles</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Particle Size</style></keyword><keyword><style  face="normal" font="default" size="100%">Sepharose</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Triazines</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">oct</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20119950</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">5</style></number><volume><style face="normal" font="default" size="100%">23</style></volume><pages><style face="normal" font="default" size="100%">462–471</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A novel magnetic support based on gum Arabic {(GA)} coated iron oxide magnetic nanoparticles {(MNP)} has been endowed with affinity properties towards immunoglobulin G {(IgG)} molecules. The success of the in situ triazine ligand synthesis was confirmed by fluorescence assays. Two synthetic ligands previously developed for binding to {IgG}, named as ligand 22/8 (artificial Protein A) and ligand 8/7 (artificial Protein L) were immobilized on to {MNPs} coated with {GA} {(MNP\_GA).} The dimension of the particles core was not affected by the surface functionalization with {GA} and triazine ligands. The hydrodynamic diameters of the magnetic supports indicate that the coupling of {GA} leads to the formation of larger agglomerates of particles with about 1 microm, but the introduction of the triazine ligands leads to a decrease on {MNPs} size. The non-functionalized {MNP\_GA} bound 28 mg {IgG/g}, two times less than bare {MNP} (60 mg {IgG/g).} {MNP\_GA} modified with ligand 22/8 bound 133 mg {IgG/g} support, twice higher than the value obtained for ligand 8/7 magnetic adsorbents (65 mg/g). Supports modified with ligand 22/8 were selected to study the adsorption and the elution of {IgG.} The adsorption of human {IgG} on this support followed a Langmuir behavior with a Q(máx) of 344 mg {IgG/g} support and K(a) of 1.5 x 10(5) M. The studies on different elution conditions indicated that although the 0.05 M citrate buffer {(pH} 3) presented good recovery yields (elution 64% of bound protein), there was occurrence of iron leaching at this acidic {pH.} Therefore, a potential alternative would be to elute bound protein with a 0.05 M {glycine-NaOH} {(pH} 11) buffer.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;{PMID:} 20119950&lt;/p&gt;
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