Appeal No. 1998-0968
Application No. 08/031,075
consideration is whether Nahm’s antibody necessarily (inherently) possesses these
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additional, undisclosed properties.
The examiner relies on Katz as extrinsic evidence that Nahm’s antibody, which
recognizes the N-acetylglucosamine hapten, inherently binds mammalian IgG. As Katz
explains, “[o]ne of the major antigenic determinants of Streptococcus Group A (Strep-A) is
N-acetyl-D-glucosamine,” and antibodies that bind the N-acetyl-D-glucosamine
determinant will “self-bind,” unless “monoclonal Anti-Streptococcal Group A antibody is
cleaved to remove the Fc portion which includes an N-acetyl-D-glucosamine moiety.”
Katz, Page 1. Similarly, the examiner relies on the present specification as evidence that
Nahm’s antibody, specific for the N-acetylglucosamine hapten, inherently binds enzyme
treated fetuin, but not native fetuin, inasmuch as “[f]etuin . . . contains N-
acetylglucosamine normally hidden in its structure,” but “[t]reatment with sialidase and
galactosidase cleaves the molecule to expose the N-acetylglucosamine.” Specification,
page 3. In our view, the extrinsic evidence relied on supports the examiner’s position, as
far as it goes.
5A recurring theme in appellants’ arguments is that “there is nothing present in
[Nahm] which suggests that [Nahm’s] monoclonal antibody has the ability to bind
mammalian cells or membranes,” and “it was initially unexpected and surprising that
monoclonal antibodies raised against the polysaccharide portion of the bacterial cell walls
of Group A Streptococci . . . would bind to mammalian cells and membranes.” Brief,
pages 18 and 19. All such arguments are irrelevant in the context of anticipation. In re
Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (When the claimed
compositions are not novel they are not rendered patentable by recitation of properties,
whether or not the properties are shown or suggested in the prior art).
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