Appeal No. 2001-0733 Page 3
Application No. 09/095,429
Louis et al. (Louis) “Autoprocessing of the HIV-1 Protease Using Purified Wild-
Type and Mutated Fusion Proteins Expressed at High Levels in Esherichia Coli,”
Eur. J. Biochem, Vol. 199 pp. 361-369 (1991)
Claims 15-22, all of the claims pending, stand rejected under 35 U.S.C.
§ 103(a) over the combination of Ardelt or Mosimann and Rybak, and over the
state of the art as exemplified by Creighton and Louis. After careful review of the
record and consideration of the issues before us, we reverse.
DISCUSSION
Claims 15-22 stand rejected under 35 U.S.C. § 103(a) as being rendered
obvious by the combination of Ardelt or Mosimann and Rybak, in view of the
state of the art as exemplified by Creighton and Louis.
Ardelt and Mosimann are cited by the rejection for teaching the amino
acid sequence of onconase, which sequence is identical to SEQ ID NO: 1.
Ardelt, according to the rejection, also teaches that cyanogens bromide
treatment of the native protein cleaves the protein into two fragments. See
Examiner’s Answer, page 8. Rybak is cited for teaching that oncanase is
currently in clinical trials for the treatment of cancer. See id. at 10.
Mosimann is also cited by the examiner for teaching the three-
dimensional structure of onconase. According to the rejection,
[t]he structure shows that the active site of the enzyme is formed
from the amino acid of Pyr-1 (pyroglutamic acid), Lys-9, His-10,
Lys-31, Thr-35, His-97 and Phe-98, see page 1149, left column,
second paragraph. Thus, any onconase missing any of these
important amino acids is expected to have compromised enzymatic
and the associated cytotoxic activity.
Id. at 9.
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