Appeal No. 2001-0762 Page 5
Application No. 08/343,585
rubredoxin analogs bind with Ni2+ to form a similar complex.” Appellants further
explain (Answer, page 7), “although Zawadzke never made the Ni2+ complex of
his rubredoxin analog, … [Saint-Martin] have made the Ni2+ complex of various
native rubredoxins, including rubredoxin isolated from D[.] desulfuricans ATCC
27774, i.e., the same rubredoxin after which Zawadzke modeled his analog….”
With regard to the rubredoxin isolate used by Zawadzke, appellants point out
(Brief, page 8) that this rubredoxin isolate has “five cysteines, four of which
participate in a ligation with Fe2+ or Fe3+ in the native state and one of which is
non-ligating.” Appellants further explain (id.), “[w]hen synthesizing his rubredoxin
analog, Zawadzke deletes the firth [sic] cysteine, ie., the non-ligating cysteine.”
The examiner recognizes that Zawadzke’s rubredoxin analog is different
from Saint-Martin’s rubredoxin in that it lacks the native N-formyl group and the
non-ligating cysteine was replaced with alanine. Answer, page 9. However, it is
the examiner’s position (Answer, bridging sentence, pages 9-10) that these
differences “are so minor that a person of ordinary skill in the art would
reasonably be expected to interpret the disclosure of Zawadzke et al. as
‘corresponding’ to native rubredoxin.” In support of this position, the examiner
finds (Answer, page 10), “the binding affinity of Fe3+ for the native and analog
rubredoxins are the same within experimental error. Both the all-L and all-D
analogs had the same binding affinity.” We note however, that Zawadzke is
silent with regard to the effect these modifications had with respect to Ni2+
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