Appeal No. 2004-0647 Page 3
Application No. 09/941,965
the present invention” (Specification, page 5), which “appears to be an intact, nearly
pure protein” (id., page 4).
Further according to the specification, “[t]his [treated] protein has independent
characteristics that are significantly different from the protein that it was derived from”
(Specification, page 4). For example,“[t]he derived protein tested negative to a
standard antigen-antibody reaction that is consistent with Bovine IgG concentrate” (id.)
and “ha[s] a significantly different molecular weight than the starting material” (id.), i.e.,
the “desired fraction . . . [has] a molecular weight of about 55,000” (id., page 5). “In
addition . . . , when used against seven enteric bacterial strains, . . . the new protein is
bacterial static when incorporated into bacterial media . . . appropriate for the test
organisms[,]” reducing “growth of the test organisms . . . from 47.5% to 99.9%
compared with controls” (id.,page 4). Similarly, “[i]n tissue cultures . . . infected with
four selected virus strains, the test protein reduced virus growth from 95% to 100%
compared with the controls” (id.). In contrast, the starting material, “when sterile filtered
and tested to determine if the intact bovine IgG was bacteria static like the acid treated
soluble fraction, . . . was not bacteria static” (id., pages 4-5). According to appellants,
treatment of the starting IgG concentrate (or fraction) “unfold[s] and modif[ies] the
protein [in the IgG concentrate], making it antimicrobial in a manner not achievable by
the original, untreated and unisolated IgG concentrate” (id., page 3).
DISCUSSION
I. Anticipation by Hatta
Claims 1, 4 and 5 stand rejected under 35 U.S.C. § 102(b) as anticipated by
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