Appeal No. 2001-1499 Page 14
Application No. 08/957,654
provided that they do not deleteriously affect IL-1 biological activity.” Column 4,
lines 52-54. Among the specifically named additives are “[p]rotease inhibitors
such as α-antitrypsin inhibitor, . . . [which] may be useful in preventing
degradation by proteolytic agents.” Column 4, lines 60-65.
Rao teaches that fibronectin (FN) participates in the repair process in skin
wounds and is “proposed to be a beneficial factor in the healing of skin wounds.”
Page 572, left-hand column. See also page 577, last paragraph: “Several
studies have demonstrated a beneficial effect for topical FN on leg ulcers.”
However, “[in] some chronic, non-healing wounds FN is extensively degraded.”
Page 572. Rao therefore “investigate[d] if serine proteases are responsible for
FN degradation in chronic skin wounds and . . . examine[d] the status of alpha1-
antitrypsin (AT) (also called α1-protease inhibitor), in acute and chronic wounds.”
Page 572, right-hand column (citation omitted). Their results “implicate[d] AT as
a regulator of FN degradation in chronic wounds. The inhibitor protects FN from
degradation by serine proteinases in chronic wounds.” Id.
Rao shows, for example, that alpha-1-antitrypsin prevents degradation of
fibronectin in vitro by proteinases from chronic wound fluid. See page 573,
paragraph bridging the columns, and the legend to Figure 6. The results showed
that alpha-1-antitrypsin protected fibronectin from degradation when added at
either 30 µg per 200 µl (equivalent to 150 µg/ml) or 120 µg per 200 µl (equivalent
to 600 µg/ml).3 See Figure 6 and page 575, paragraph bridging the columns.
3 When describing the difference between the lanes shown in the Figure, Rao refers to lanes 3
and 4 as showing degradation in the presence of “5 µg” and “20 µg,” respectively. These
numbers apparently reflect the absolute amount (not concentration) of alpha-1-antitrypsin in the
samples; only a portion of each sample was immunoblotted. See the legend to Figure 6.
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