Purification and quantities of immunoglobulins of rheumatoid synovial tissues.

Synovial tissue of rheumatoid arthritic origin was incubateed with radio-labelled amino acids and the immunoglobulin fraction of the products isolated using either a diethylaminoethyl (DEAE)-cellulose column or an affinity column of antihuman immunoglobulin coupled to Sepharose. The affinity column method provided a simple, one-step procedure for obtaining quantitative yields of substantially pure immunoglobulin. The elutions from the affinity columns utilized guanidine-HCl allowing the elutions to be performed quickly and under conditions which apparently did not denature the immunoglobulins except perhaps immunoglobulin M. Other solvent conditions for dissociating antibody-antigen complexes were shown to be not suitable and resulted in large volumes of eluates. The affinity columns could be reutilized many times without apparent loss of capacity to bind immunoglobulins.