Chromatographic kinetic measurements of human serum albumin adsorption on monoclonal antibodies.

A chromatographic method was employed to study the kinetics of human serum albumin (HSA) adsorbed on immobilized monoclonal antibodies. The antibodies of various specificities were covalently bound to a high-performance liquid chromatography (HPLC) silica support. For very low desorption rates, successive amounts of the reacting protein were injected until column saturation.

[Study of albumin conformational changes in human serum using an immunoenzymatic technic using monoclonal antibodies].

The specificity of six peroxidase-labelled anti-albumin monoclonal antibodies was studied by allowing them to react with albumin-derived fragments of known structure comprising the whole albumin molecule. The epitopes corresponding to these antibodies were located on defined regions of the albumin molecule extending from the N to the C-terminal ends. These antibodies have been used for investigating by ELISA the conformational alterations of albumin molecule brought about by the N-B transition in twelve individual sera.

Enzyme immunoassay using monoclonal antibodies to study conformational changes of human serum albumin.

A method for studying conformational changes induced in the human albumin molecule, either in its purified form or in serum, is described. Plates were coated with albumin or human serum at varying pHs and were reacted with peroxidase-labeled anti-albumin monoclonal antibodies of different specificities. The data showed that albumin molecules were coated in conformations induced as a result of pH changes, allowing us to demonstrate that pH modifications involved the N-terminal portion of the albumin molecule whether in its purified form or in serum.