Appeal No. 2002-1874 Page 7
Application No. 09/079,329
Claims 47-49, 54-56 and 237-244 stand rejected under 35 U.S.C.
§ 103(a) as being obvious over Selwood or Lo as combined with the admitted
prior art.
Selwood and Lo are cited by the rejection for teaching that methylglyoxal
covalently binds to blood proteins such as albumin, irreversibly modifying them,
and that arginine and N-a-acetyl arginine inhibit that binding by competing for
binding to methylglyoxal. The rejection than cites the specification for teaching
that “[i]t is known . . . that accumulation of toxic reactive carbonyl compounds is
related to some various disorders, e.g, diabetes mellitus, cataract, and kidney
disorders,” and that “[t]he carbonyl compounds may be sugar-derived, such as
glyoxal, methylglyoxal or their derivatives,”
The Answer concludes:
It would have been obvious to one skilled in the art at the
time the invention was made to be motivated to use arginine or its
derivatives to prevent undesired modification of albumin and other
blood proteins by methylglyoxal because it is known in the art that
accumulation of methylglyoxal is related to development of various
disorder conditions and because Selwood and Lo teach that
arginine and its derivatives inhibit interaction of albumin with
methylglyoxal. One would be motivated to remove methylglyoxal
from blood circulation as the primary site of its accumulation, and,
to achieve that, one would be motivated to deliver arginine into
blood either by administration of arginine, or by treatment of blood
during blood dialysis, which is a routine procedure for removal of
unnecessary contaminations from blood (see, e.g, references listed
on p.19, lines 18-26, of the instant specification). One would be
motivated to use arginine as methylglyoxal scavenger to preserve
albumin and other blood protein from interaction with methylglyoxal
scavenger to preserve albumin and other blood protein from
interaction with methylglyoxal because methylglyoxal may cause
albumin modification and may cause albumin gelatinization, and
preserving the blood proteins from such modifications is a desired
effect
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