Appeal No. 94-1573 Paper No. 24
Application No. 07/552,744 Page 2
incapable of de novo purine synthesis within the red blood
cells of the host and must rely upon the host's cells as a
source for needed purines (Paper No. 1 at 1 and 2).
The P. falciparum enzyme hypoxanthine-guanine
phosphoribosyl transferase (HGPRT) is present in blood-stage
P. falciparum parasites at high levels. The enzyme scavenges
purines from host cells to form nucleotides for the parasites'
own use. Specifically, the enzyme catalyzes the
phosphoribosylation of hypoxanthine and guanine to yield the
nucleotides inosine monophosphate (IMP) and guanosine (Paper
No. 1 at 2 and 3).
Appellants report that they have isolated the cDNA
sequence of the protein Plasmodium falciparum HGPRT and have
successfully expressed this protein in E. coli (Paper No. 1
at 6 and 7).
The rejections
The examiner made the following rejections:
1. Claims 2-4 and 6 under 35 U.S.C. § 102(a) as
anticipated by-
G. Vasanthakumar, R.L. Davis, Jr., M.A. Sullivan, &
J.P. Donahue, Nucleotide sequence of cDNA clone for
hypoxanthine-guanine phosphoribosyltransferase from
Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 13 14 Next
Last modified: November 3, 2007