%0 Journal Article %1 citeulike:693757 %A Scheuermann, J. %A Viti, F. %A Neri, D. %C Institute of Pharmaceutical Sciences, Swiss Federal Institute of Technology, ETHZ, Winterthurerstrasse 190, CH-8057, Zurich, Switzerland. %D 2003 %J J Immunol Methods %K affinity antibody elisa kinetic %N 1-2 %P 129--134 %T Unexpected observation of concentration-dependent dissociation rates for antibody-antigen complexes and other macromolecular complexes in competition experiments. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12738365 %V 276 %X The dissociation rate constant of bimolecular complexes between macromolecules (k(off)) is often measured in solution by competition experiments and is generally expected to follow first-order kinetics.When measuring k(off) constants by competition for three complexes of high-affinity recombinant antibody fragments with the cognate antigen and for one calmodulin/peptide complex, a surprising dependence between apparent dissociation rate and concentration of competitor (antigen or calmodulin-binding peptide) was observed.Our results may be characteristic for macromolecules consisting of two domains (such as single-chain Fv fragments) and may reflect a transient opening of the two domains which are involved in the binding reaction, and which are connected by a polypeptide linker.

@article{citeulike:693757, abstract = {The dissociation rate constant of bimolecular complexes between macromolecules (k(off)) is often measured in solution by competition experiments and is generally expected to follow first-order kinetics.When measuring k(off) constants by competition for three complexes of high-affinity recombinant antibody fragments with the cognate antigen and for one calmodulin/peptide complex, a surprising dependence between apparent dissociation rate and concentration of competitor (antigen or calmodulin-binding peptide) was observed.Our results may be characteristic for macromolecules consisting of two domains (such as single-chain Fv fragments) and may reflect a transient opening of the two domains which are involved in the binding reaction, and which are connected by a polypeptide linker.}, added-at = {2006-07-07T01:10:50.000+0200}, address = {Institute of Pharmaceutical Sciences, Swiss Federal Institute of Technology, ETHZ, Winterthurerstrasse 190, CH-8057, Zurich, Switzerland.}, author = {Scheuermann, J. and Viti, F. and Neri, D.}, biburl = {https://www.bibsonomy.org/bibtex/27ee135b641e3e515aef1420655b4d090/biblio24}, citeulike-article-id = {693757}, interhash = {2bfb780c7be1868aeb32eddb5acc51fa}, intrahash = {7ee135b641e3e515aef1420655b4d090}, issn = {0022-1759}, journal = {J Immunol Methods}, keywords = {affinity antibody elisa kinetic}, month = May, number = {1-2}, pages = {129--134}, priority = {2}, timestamp = {2006-07-07T01:10:50.000+0200}, title = {Unexpected observation of concentration-dependent dissociation rates for antibody-antigen complexes and other macromolecular complexes in competition experiments.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=12738365}, volume = 276, year = 2003 }