Appeal No. 1997-0483
Application No. 07/648,900
appellants and the examiner. We make reference to the examiner's answer (Paper No.
37, mailed March 5, 1996) for the examiner's reasoning in support of the rejections and to
the appellants' brief (Paper No. 36, filed November 13, 1995) and to appellants' reply brief
(Paper No. 39, filed May 13, 1996) for the appellants' arguments thereagainst.
BACKGROUND
Thrombomodulin is an endothelial cell surface glycoprotein that forms a high affinity
complex with thrombin wherein the clotting activity of thrombin is inhibited.
Thrombomodulin is organized into five regions: (1) an amino terminal, hydrophobic region
(residues 1-244); (2) a cysteine-rich region containing six repeated structures homologous
to the epidermal growth factor precursor, called EGF-like or EGF-homology domains
(residues 245-480); (3) a serine/threonine/proline-rich region with O-glycosylation sites
(residues 481-514); (4) a hydrophobic transmembrane region (residues 515-537); and (5)
a cytosolic tail (residues 538-575). As shown in Figure 6, the residues of the cysteine-rich
region can be separated into three fragments by cyanogen bromide digestion, i.e., CB-1,
CB-2 and CB-3, beginning at residues 234, 310 and 407, respectively. [Specification, p.
1, para. 3; p. 2, para. 2-3; p. 3, penultimate para.; Figure 6; p. 5, para. 2.]
The claimed invention is directed to polypeptides derived from thrombomodulin and
their use in inhibiting coagulation (brief, p. 2, last para.).
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