Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2004-06-29
2010-11-02
Nashed, Nashaat (Department: 1656)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S068100, C435S252300, C435S252330, C435S252340, C435S252350, C435S254110, C435S358000, C536S023400
Reexamination Certificate
active
07824885
ABSTRACT:
The present invention is directed to the identification of a protease prodomain that is capable of binding a corresponding protease with high affinity. The protease prodomain of the present invention is fused to a second protein to form a protease prodomain fusion protein. The presence of a protease prodomain protein in a fusion protein allows for easy and selective purification of the second protein by incubation with the corresponding protease.
REFERENCES:
patent: 4980288 (1990-12-01), Bryan et al.
patent: 4990452 (1991-02-01), Bryan et al.
patent: 5013657 (1991-05-01), Bryan et al.
patent: 5116741 (1992-05-01), Bryan et al.
patent: 5246849 (1993-09-01), Bryan et al.
patent: 5260207 (1993-11-01), Pantoliano et al.
patent: 5371008 (1994-12-01), Carter et al.
patent: 5371190 (1994-12-01), Carter et al.
patent: 5470733 (1995-11-01), Bryan et al.
patent: 5567601 (1996-10-01), Bryan et al.
patent: 5652136 (1997-07-01), Carter et al.
patent: 5707848 (1998-01-01), Bryan et al.
patent: 6541234 (2003-04-01), Bryan
patent: 6541235 (2003-04-01), Bryan
patent: 7098002 (2006-08-01), Rubinstein et al.
patent: 7531325 (2009-05-01), Van Rooijen et al.
patent: 2003/0166162 (2003-09-01), Van Rooijen et al.
Gron, H., et al., 1992, “Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching”, Biochemistry, vol. 31, pp. 6011-6018.
Gron, H., et al., 1996, “Studies of binding sites in the subtilisin fromBacillus lentusby means of site directed mutagenesis and kinteic investigations”, in Subtilisin Enzymes: Practical Protein Engineering, pp. 105-112, Bott, R., and Betzel, C., Eds., Plenum Press, New York.
Strausberg, S.L., et al., 2005, “Directed coevolution of stability and catalytic activity in calcium-free subtilisins”, Biochemistry, vol. 44, No. 9, pp. 3272-3279.
Strauberg, S., et al., 1993, “Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment”, Biochemistry, vol. 32, pp. 8112-8119.
Ohta, Y., et al., 1991, “Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide”, Molecular Microbiology, 5(6): 1507-1510.
Egnell, P., et al., 1991, “The subtilisin Carlsberg pro-region is a membrane anchorage for two fusion proteins produced inBacillus subtilis”, Gene, 97(1): 49-54.
Jordan, F., et al., 1993, “Proton NMR of the active center of serine proteases complexed to slow- and rapid-binding inhibitors and to the pro-peptide of subtilisin E, a protein-protease inhibitor”, Journal of Cellular Biochemistry Supplement, 0(17) Part C: p. 295, Abstract No. LZ 425.
Strausberg, S., et al., 1993, “Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment”, Biochemistry, 32(32): 8112-8119.
Hu, Z., et al., 1996, “Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin”, Journal of Biological Chemistry, 271(7): 3375-3384.
Volkov, A., et al., 1996, “Evidence for intromolecular processing of prosubtilisin sequestered on a solid support”, Journal of Molecular Biology, 262: 595-599.
Fu, X., et al., 2000, “Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked”, Journal of Biological Chemistry, 275(22): 16871-16878.
Kojima, S., et al., 2001, “Accelerated refolding of subtilisin BPN' by tertiary-structure-forming mutants of its propeptide”, Journal of Biochemistry, 130(4): 471-474.
Marie-Claire, C., et al., 2001, “Folding Pathway Mediated by an Intramolecular Chaperone: The Structural and Functional Characterization of the Aqualysin I Propeptide”, Journal of Molecular Biology, 305(1): 151-165.
Chowdhury, S. F., et al., 2002, “Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides”, Journal of Medicinal Chemistry, 45(24): 5321-5329.
Yabuta, Y., et al., 2003, “Folding Pathway Mediated by an Intramolecular Chaperone”, Journal of Biological Chemistry, 278(17): 15246-15251.
Abdulaev, N. G., et al., 2005, “Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein-subunit”, Journal of Biomolecular NMR, 32(1): 31-40.
Baier, K. et al., “Evidence for propeptide assisted folding of calcium dependent protease of the cyanobacterium Anabaena”, “European Journal of Biochemistry”, Aug. 1996, pp. 750-755, vol. 241.
Bech, L. M. et al. , “Mutational replacements in substilisin 309”, “European Journal of Biochemistry”, May 1, 1992, pp. 869-874, vol. 209.
Bech, L. M. et al. , “Significance of Hydrophobic S4-P4 Interactions in Subtilisin 309 fromBacillus”, “Biochemistry”, Jan. 1993, pp. 2845-2852, vol. 32, No. 11.
Bryan, P. et al., “Energetics of Folding Subtilisin BPN'”, “Biochemistry”, Apr. 1, 1992, pp. 4937-4945, vol. 31, Publisher: American Chemical Society.
Bryan, P. et al., “Catalyis of a Protein Folding Reaction: Mechanistic Implications of the 2.0 A”, “Biochemistry”, Jun. 1995, pp. 10310-10318, vol. 34, Publisher: American Chemical Society.
Bryan, P. et al., “Prodomains and protein folding catalysis”, “Chem. Rev.”, 2002, pp. 4805-4816, vol. 102, No. 12.
Cao, J. et al., “The Propeptide Domain of Membrane Type 1-Matrix Metalloproteinase Acts as an Intramolecular Chaperone when Expressed in”, “Journal of Biological Chemistry”, Sep. 22, 2000, pp. 29648-29653, vol. 275, No. 38.
Carter, P. et al., “Engineering enzyme specificity by ‘substrate-assisted catalysis’”, “Science”, Jul. 24, 1987, pp. 394-399, vol. 237, No. 4813.
Carter, P. et al., “Dissecting the catalytic triad of a serine protease”, “Nature”, Apr. 7, 1988, pp. 564-568, vol. 332.
Cawley, Niamh X. et al., “Activation and Processing of Non-anchored Yapsin 1 (Yap3p)”, “J. Biol. Chem.”, Jan. 2, 1998, pp. 584-591, vol. 273, No. 1.
Craik, C. et al., “The Catalytic Role of the Active Site Aspartic Acid in Serine Proteases”, “Science”, Aug. 21, 1987, pp. 909-913, vol. 237, No. 4817.
Estell, D.A. et al., “Probing Steric and Hydrophobic Effects on Enzyme-Substrate Interactions by Protein”, “Science”, Aug. 8, 1986, pp. 659-663, vol. 233, No. 4746.
Fabre, E. et al., “Role of the Proregion in the Production and Secretion of the Yarrowia lipolytica Alkaline Extracellular Protease”, “The Journal of Biological Chemistry”, Feb. 25, 1991, pp. 3782-3790, vol. 266, No. 6.
Fukuda, R. et al., “The Prosequence of Rhizopus niveus Aspartic Proteinase-1Supports Correct Folding and Secretion of Its Mature Part in Sac”, “The Journal of Biological Chemistry”, Apr. 1, 1994, pp. 9556-9561, vol. 269, No. 13.
Gallagher, T.D. et al., “The prosegment-subtilisin BPN' complex: crystal structure of a specific ‘foldase’”, “Structure”, Sep. 15, 1995, pp. 907-914, vol. 3, No. 9.
Gron, Hanne, et al., “Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are . . . ”, “Biochemistry”, 1992, pp. 6011-6018, vol. 31.
Gron, Hanne, et al., “Studies of binding sites in the subtilisin fromBacillus lentusby means of site directed mutagenesis and kinetic . . . ”, “Subtilisin Enzymes: Practical Protein Engineering”, 1996, pp. 105-112, Publisher: Plenum Press, Published in: New York.
Gron, Hanne, et al.,
Hultquist Steven J.
Intellectual Property / Technology Law
Moore William W
Nashed Nashaat
Reynolds Kelly K.
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