Interference No. 102,572
time of work are not fully explained. These pages are illegible and also contain
unexplained attachments.
Cabilly et al., in their brief, page 16, argue that the SDS-PAGE gel run by Mumford
showed that each of these transformants, GGLH-1 and GGLH-2, was expressing both
heavy and light chains. (our emphasis). They also argue in their reply brief, page 17, that
Mumford testified that:
“Analysis by SDS-polyacrylamide gel electrophoresis (PAGE) show[ed] a
band in the 55kD region which is the expected molecular weight of the heavy
chain product,” (Mumford, CR-37,¶10) “ SDS-PAGE analysis indicated
product expression at the 23.5kD molecular weight range which was
expected for light chain product,” (Mumford, CR37-38, ¶12) and then finally
that SDS-PAGE showed that the cotransformed cells expressed both the
heavy and light chain of the antiCEA-antibody.(our emphasis)
Initially we note that this record never identifies the origin of GGLH-1 and GGLH-2,
that is, who made them, the process used to make them, and what DNA they contained.
Contrary to the Cabilly et al. arguments, Mumford never testified that the SDS-PAGE gel
of GGLH-1 and GGLH-2 showed expression of both the heavy and light chain(our
26 27
emphasis). Mumford testified to an expectation and not to what he actually found. The
26Mumford actually stated: [T]he products that were expected from these
fermentation runs were both the light and heavy chain of an anti-CEA antibody. SDS-
PAGE shows protein expression from the time course samples. I recorded that the
fermentation run No. GGLH-1 was harvested and that the 80 grams of wet biomass paste
was given to Dr. Ron Wetzel. Fermentation GGLH-1 demonstrated refractile bodies upon
microscopic analysis. (¶ 13). (CR-38).
27Mumford’s entry in his notebook No. 18, at page 31 (Bates 730) actually appears
to contradict the Cabilly et al. arguments. Mumford states (as best that we can read the
(continued...)
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