p.18
E.S. Ward, D. Güssow, A.D. Griffiths, P.T. Jones, G. Winter, "Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli," Nature, 341:544-46, 1989.
Sally Ward (University of Texas Southwestern Medical Center, Dallas): "This paper describes the isolation and characterization of immunoglobulin heavy chain variable domains (VHs) that have antigen-binding activities.
"The initial observation that the VH domain derived from an antilysozyme (D1.3) mono-clonal antibody has high affinity for antigen binding, in the absence of a paired light chain variable domain, has been extended to the generation and analysis of VH domain repertoires. The polymerase chain reaction has been used to isolate diverse repertoires of VH domains from the spleen DNA of mice that have been hyperimmunized with antigen (lysozyme or keyhole-limpet haemocyanin). The VH domains have been expressed as secreted proteins in Escherichia coli, and clones producing VHs with antigen-binding activities have been identified by ...
