Appeal No. 1996-1085
Application No. 08/097,621
Claim 32 is illustrative of the subject matter on appeal and is reproduced
below:
32. A process for increasing the formation of the natural protein
conformation when disulfide bonded proteins are secreted by an E.coli
host that contains a recombinant DNA coding for the secreted protein,
comprising culturing the host in a suitable culture medium in the
presence of oxygen under conditions suitable for the expression of the
recombinant DNA, wherein said culture medium contains 0.1 to 20
mmol/l of one or more thiol reagents.
The references relied upon by the examiner are:
Pigiet et al. (Pigiet) 4,904,602 February 27, 1990
Bowden et al. (Bowden), “Folding and Aggregation of J-Lactamase in the
Periplasmic Space of Escherichia coli,” The Journal of Biological Chemistry, Vol.
265, No. 28, pp. 16760-766 (1990)
Hiram F. Gilbert (Gilbert), Advances in Enzymology, Vol. 63, pp. 70-74, and 144-
46 (Alton Meister ed. , John Wiley & Sons 1990)
Appellants rely on the following references:
Wetlaufer et al. (Wetlaufer), “The oxidative folding of proteins by disulfide plus thiol
does not correlate with redox potential,” Protein Engineering, Vol. 1, No. 2, pp. 141-
46 (1987)
Gething et al., “Protein folding in the cell,” Nature, Vol. 355, pp.33-45 (1992)
Bardwell et al., “A pathway for disulfide bond formation in vivo,” Proc. Natl. Acad.
Sci. USA, Vol. 90, pp. 1038-1042 (1993)
Missiakas et al. (Missiakas), “Identification and characterization of the Escherichia
coli gene dsbB, whose product is involved in the formation of disulfide bonds in
vivo,” Proc. Natl. Acad. Sci. USA, Vol. 90, pp. 7084-088 (1993)
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