Appeal No. 2006-2556 Page 3
Application No. 09/977,155
C-terminal tail, and (ii) a protease which specifically cleaves the domain and
thereby releases the tail from the membrane;
b) incubating the sample under conditions wherein the protease cleaves
the domain and thereby releases the tail from the membrane; and
c) detecting a resultant released tail, which indicates proteolysis of the
LDL receptor transmembrane domain.
15. A method according to claim 1, wherein the LDL receptor is LRP1b and
the protease is native to the membrane.
Thus, claim 1 is directed to a method for assaying the proteolysis of an LDL
receptor transmembrane domain by detecting the release of the C-terminal tail from the
remainder of the membrane-bound protein.
The method involves incubating a cell membrane that contains a protease and
an LDL receptor transmembrane domain fused to a C-terminal tail, under conditions that
allow the protease to cleave the transmembrane domain and release the C-terminal tail
from the membrane. Detection of the released tail indicates that the proteolytic
cleavage has occurred.
Claim 15 limits the process of claim 1 to one in which a specific LDL receptor
(LRP1b) is cleaved and the protease is one that is native to the membrane.
2. Anticipation by Willnow
Claims 1-9 and 11-14 stand rejected under 35 U.S.C. § 102(b) as being
anticipated by Willnow.1
The examiner points out that Willnow teaches “methods involving LRP-
mini[]receptors,” which are truncated versions of the low density lipoprotein receptor-
1 Willnow et al., “Molecular Dissection of Ligand Binding Sites on the Low Density Lipoprotein Receptor-
related Protein,” The Journal of Biological Chemistry, Vol. 269, No. 22, pp. 15827-15832 (1994).
Page: Previous 1 2 3 4 5 6 7 8 9 10 Next
Last modified: November 3, 2007