Appeal No. 2002-1479 Page 7
Application No. 08/794,042
(2) a nonglycosylated molecular weight of 23,000 (page 1682, right-hand
column);
(3) 222 total amino acids (page 1680, right-hand column); and
(4) an amino acid composition that includes 23 aspartic acid residues and
14 leucine residues per molecule of protein (Table III).
None of these properties are shared by the instantly claimed enterokinase
light chain:
(1) The glycosylated molecular weight of the claimed enzyme is 42,000
daltons (specification, pages 13 and 20), while the glycosylated
molecular weight of the prior art enzyme is 35,000 daltons.
(2) The calculated molecular weight of the instant protein is 26,262 (see
LaVallie, page 23316),2 while the calculated molecular weight of the
prior art enzyme is 23,000 daltons.
(3) Claim 42 is directed to an enterokinase light chain that comprises
amino acids 564 to 798, inclusive, of SEQ ID NO:2. Thus, the
claimed enzyme has 235 amino acids, while the prior art enzyme is
disclosed to have 222 amino acids.
(4) Amino acids 564 to 798 of SEQ ID NO:2 include 11 aspartic acid
residues and 18 leucine residues (Reply Brief, page 8; see also
Figure 2), while the prior art enzyme includes 23 aspartic acids and 14
leucines.
In addition, as Appellant points out, the prior art enzyme was isolated from
bovine duodenal mucosal cells (Liepnieks) or mucosal fluid (Fonseca, Light),
while the instant specification states that “[b]ovine enterokinase (EK-2 grade)
was purchased from Biozyme . . . [and] further purified using porcine pancreatic
trypsin inhibitor (Sigma) coupled to activated SEPHAROSE CL-4B.” Page 13.
2 The enterokinase light chain amino acid sequence taught by LaVallie (Figure 2) appears to be
the same as that of that of amino acids 564-798 of instant SEQ ID NO:2. Therefore, the
calculated molecular weight disclosed by LaVallie would also appear to apply to the instantly
claimed enzyme.
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