Appeal No. 2000-0630 Application No. 07/780,717 Claims 39, 58 and 68 are representative of the claims on appeal and read as follows: 39. A method of making a recombinant bifunctional streptavidin-metallothionein chimeric protein, said method comprising steps: (a) introducing into a host cell a nucleic acid encoding a bifunctional fusion protein comprising a streptavidin moiety and a metallothionein moiety, wherein said streptavidin moiety consists of residues 16 to 133 (SEQ ID N0:7) of mature streptavidin; (b) incubating said cell under conditions sufficient to express said fusion protein; (c) isolating said fusion protein. 58. A bifunctional recombinant streptavidin-metallothionein chimeric protein, wherein said protein comprises a streptavidin moiety and a metallothionein moiety, and said streptavidin moiety consists of residues 16 to 133 (SEQ ID N0:7) of mature streptavidin. 68. A functional streptavidin consisting of residues 16 to 133 (SEQ ID N0:7) of mature streptavidin. The examiner relies on the following references: Tolman 4,732,864 Mar 22, 1988 Rodwell et al. (Rodwell) 5,196,510 Mar. 23, 1993 Meade et al. (Meade) WO 8,602,077 Apr. 10, 1986 Kenten et al. (Kenten) WO 8,909,393 Oct. 5, 1989 Shoemaker et al. (Shoemaker) WO 9,006,323 Jun. 14,1990 Hendrickson et al. (Hendrickson), “Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation,” Proc. Natl. Acad. Sci. USA, Vol. 86, pp. 2190-2194 (April 1989) Lowenadler et al. (Lowenadler), “A gene fusion system for generating antibodies against short peptides,” Gene, Vol. 58, pp. 87-97 (1987) Sano et al. (Sano), “Expression of a cloned streptavidin gene in Escherichia coli,” Proc. Natl. Acad. Sci. USA, Vol. 87, pp. 142-146 (January 1990) 2Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 NextLast modified: November 3, 2007