<?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%">Conrath, K.</style></author><author><style face="normal" font="default" size="100%">Pereira, A. S.</style></author><author><style face="normal" font="default" size="100%">Martins, C. E.</style></author><author><style face="normal" font="default" size="100%">Timoteo, C. G.</style></author><author><style face="normal" font="default" size="100%">Tavares, P</style></author><author><style face="normal" font="default" size="100%">Spinelli, S.</style></author><author><style face="normal" font="default" size="100%">Kinne, J.</style></author><author><style face="normal" font="default" size="100%">Flaudrops, C.</style></author><author><style face="normal" font="default" size="100%">Cambillau, C.</style></author><author><style face="normal" font="default" size="100%">Muyldermans, S.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Tegoni, M.</style></author><author><style face="normal" font="default" size="100%">Desmyter, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase</style></title><secondary-title><style face="normal" font="default" size="100%">Protein Sci</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibody Affinity</style></keyword><keyword><style  face="normal" font="default" size="100%">Camelids, New World/*immunology</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallography, X-Ray</style></keyword><keyword><style  face="normal" font="default" size="100%">Epitope Mapping</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin Fragments/immunology</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin Heavy Chains/immunology</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidoreductases/*immunology</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptide Library</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword><keyword><style  face="normal" font="default" size="100%">Surface Plasmon Resonance</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Mar</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=19241371 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">619-28</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Nitric Oxide Reductase (NOR) is an integral membrane protein performing the reduction of NO to N(2)O. NOR is composed of two subunits: the large one (NorB) is a bundle of 12 transmembrane helices (TMH). It contains a b type heme and a binuclear iron site, which is believed to be the catalytic site, comprising a heme b and a non-hemic iron. The small subunit (NorC) harbors a cytochrome c and is attached to the membrane through a unique TMH. With the aim to perform structural and functional studies of NOR, we have immunized dromedaries with NOR and produced several antibody fragments of the heavy chain (VHHs, also known as nanobodies). These fragments have been used to develop a faster NOR purification procedure, to proceed to crystallization assays and to analyze the electron transfer of electron donors. BIAcore experiments have revealed that up to three VHHs can bind concomitantly to NOR with affinities in the nanomolar range. This is the first example of the use of VHHs with an integral membrane protein. Our results indicate that VHHs are able to recognize with high affinity distinct epitopes on this class of proteins, and can be used as versatile and valuable tool for purification, functional study and crystallization of integral membrane proteins.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">19241371</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;1469-896X (Electronic)0961-8368 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Laboratory of Cellular and Molecular Immunology, Vrije Universiteit Brussel, Brussels, Belgium.</style></auth-address></record></records></xml>