Appeal No. 2004-2134 Page 4
Application No. 09/425,075
then transformed with these constructs, and the resulting
transformant secretes functionally assembled intact recombinant
antibody molecules into the medium from where it is readily
recovered using affinity purification procedures.
Specificity of the produced antibody is determined by
demonstrating the antibody-specific mRNA synthesis in
recombinant yeast using Northern blot analysis. When the specific
antibody is produced, immunoblot and ELISA analyses of
concentrated culture supernatants harvested a few days post-
transformation reveal the presence of antigen-specific human,
mouse or other mammalian species-specific immunoglobulins.
Assaying of the culture supernatants by ELISA then shows specific
binding activity to the specific antigen against which the antibody is
raised or to a crossreactive congener. The binding affinity of the
produced recombinant IgG is the same as, and/or comparable to,
that of the parent IgG.
Id. at 6-7.
DISCUSSION
Claims 36-39 and 42-50 stand rejected under 35 U.S.C. § 103(a) as being
rendered obvious by the combination of Horwitz, Cregg, the Invitrogen Catalog
and Robinson. As the claims stand or fall together, see Appeal Brief, page 7, we
focus our analysis on the method of claim 36.
Horwitz is cited for teaching a method “for the production of an antibody in
S. cerevisiae yeast cells with the vectors comprising cDNA encoding for an
antibody, a promoter and transcription terminator, and signal sequence.”
Examiner’s Answer, page 4. According to the rejection, “Horwitz [ ] does not
teach a recombinant host P. pastoris, SMD1168 transformed with a vector for
expression with dual expression cassettes, the Pichia alcohol oxidase promoter,
alpha factor signal sequence, AOX1-P promoter.” Id.
Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 Next
Last modified: November 3, 2007