Appeal No. 2001-2379 Page 2
Application No. 08/931,666
The examiner relies on the following references:
Abrams et al. (Abrams), ”Optimal Strategies for Developing Human-Human
Monoclonal Antibodies,” Methods in Enzymology, Vol. 121, pp. 107-119 (1986)
Barone et al. (Barone), ”Reactivity of E. coli-derived trans-activating protein of
human T lymphotropic virus Type III with sera from patients with acquired
immune deficiency syndrome,” The Journal of Immunology, Vol. 137, No. 2,
pp. 669-673 (1986)
Triguero et al. (Triguero), ”Blood-brain barrier transport of cationized
immunoglobulin G: Enhanced delivery compared to native protein,” Proc. Natl.
Acad. Sci. USA, Vol. 86, pp. 4761-4765 (1989)
Fahey et al. (Fahey), ”Status of immune-based therapies in HIV infection and
AIDS,” Clin. exp. Immunol., Vol. 88, pp. 1-5 (1992)
Fox, No winners against AIDS,” Bio/Technology, Vol. 12, p. 128 (1994)
Claims 1-15 stand rejected under 35 U.S.C. § 112, first paragraph, as not
enabled by the specification.
Claims 1-15 stand rejected under 35 U.S.C. § 103 as obvious in view of
Triguero, Barone, and Abrams.
We reverse both rejections.
Background
“Most antibodies have an isoelectric point of between about 5 to 6.”
Specification, page 6. “Cationization involves substituting basic groups in place
of a sufficient number of surface carboxyl groups to increase the pI of the
antibody to between 8.0 to 11.0.” Id. “Cationization of proteins is known, in
general, to enhance their cellular uptake. The prior art teaches that the uptake of
cationized proteins is by endocytosis. . . . [P]roteins which are taken up by this
method are sequestered in intracellular compartments.” Id., page 5.
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