Appeal No. 1995-2903
Application No. 07/693,055
a viral antibody, as the binding material, to bind viral glycoprotein to the assay surface.
The examiner acknowledges at page 7 of the Answer that:
NEURATH does not teach the use of a solid support that has been coated
with a lectin where on said coated support the lectin serves as the binding
member for the immobilization of viral glycoproteins.
The examiner relies on Larson as teaching (Answer, page 7):
that (a) lectins are to be utilized in the (purification) immobilization of viral
glycoproteins to a surface; (b) the selection of the appropriate lectin is a
process known to those skilled in the art; and (c) the use of lectins results in
the immobilization of viral glycoproteins that are free of detectable double
stranded DNA and can be further utilized as a vaccine.
The examiner acknowledges that Larson (Answer, page 8):
does not teach of the detection of antibodies which bind to the immobilized
viral glycoproteins . . . .
The examiner determines that (Answer, paragraph bridging pages 8-9):
. . . the lectin in the affinity-purification taught by LARSON is used for the
same purpose as the antibody in the immunoassay taught by NEURATH,
that being the immobilization of a solubilized viral glycoprotein to a coated
support. Accordingly, the lectin and the antibody which are used to
immobilize solubilized viral glycoproteins to a support would have been
considered interchangeable.
The examiner then concludes that (Answer, paragraph bridging pages 9-10):
it would have been obvious to one of ordinary skill in the art at the time the
invention was made to have (1) coated a solid support with a lectin with the
intent to immobilize viral glycoproteins thereon as taught by LARSON; (2) to
have prepared the immobilized viral glycoproteins in a manner by which they
were first treated with a detergent such as Triton X and Nonidet P-40 as
taught by LARSON; (3) immobilized viral glycoproteins on a lectin-coated
surface; and (4) to have combined the now immobilized viral glycoproteins in
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