>> have developed an improved method for Epstein-Barr virus transformation <<
Guess I need to read the manuscript...... nothing new about deriving human MAbs from EBV transformation. Tony Siadak, Mae Rosok, Mark Lostrom et al. at Genetic Systems (subsequently Oncogen, subsequently Bristol-Myers Squibb Research Institute) -- sent us great antibody-producing lines. We at Cutter (Bayer) scaled them up, characterized the protective capacity, etc. Sorry, no publications from my group or from GS at the time. There are some patents and applications that I could dig out. But Gloria Meng did report to me and published this work that we were doing when I left......
Eur J Immunol. 1990 Nov;20(11):2505-8.
J chain deficiency in human IgM monoclonal antibodies produced by Epstein-Barr virus-transformed B lymphocytes.
Meng YG, Criss AB, Georgiadis KE.
Cutter Biological, Miles Inc., Berkeley, CA 94701.
Six human IgM monoclonal antibodies against Pseudomonas aeruginosa were purified and characterized. On agarose-acrylamide sodium dodecyl sulfate (SDS) gels run under nonreducing conditions, IgM monoclonal antibodies showed variable amounts of a slower migrating form of IgM in addition to the one co-migrating with plasma IgM. Protein blotting with anti-J chain antibody showed that the slower migrating form did not contain J chain. Analysis of one of the monoclonal antibodies by sucrose gradient centrifugation showed that the J chain-deficient form sedimented faster than the complete IgM. It is known that IgM preparations lacking J chain sediment faster by sucrose gradient centrifugation analysis and tend to form hexamers. The slower migrating form of IgM we observed on SDS gels under nonreducing conditions could be hexameric IgM. Further evaluation of this monoclonal antibody demonstrated that both forms of IgM had the same antigen-binding activity. Glycosylation of the light chain was demonstrated in two of the monoclonal antibodies. |
