Animal product free media and processes for obtaining a...

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Using a micro-organism to make a protein or polypeptide

Reexamination Certificate

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C435S252700, C435S253600, C435S842000, C424S236100, C424S239100

Reexamination Certificate

active

08008044

ABSTRACT:
Media and processes for the fermentation ofClostridium botulinumand obtaining a botulinum toxin for use in formulating botulinum toxin pharmaceutical compositions. The growth media can contain significantly reduced levels of meat or dairy by-products using non-animal based products to replace the animal-derived products. Preferably, the media used are substantially free of animal derived products.

REFERENCES:
patent: 4401683 (1983-08-01), Thompson
patent: 5902565 (1999-05-01), Cox et al.
patent: 6558926 (2003-05-01), Demain et al.
patent: 6818409 (2004-11-01), Oguma
patent: 7148041 (2006-12-01), Donovan
patent: 7160699 (2007-01-01), Wang et al.
patent: 7189541 (2007-03-01), Donovan
patent: 7354740 (2008-04-01), Xiang et al.
patent: 7445914 (2008-11-01), Donovan
patent: 7452697 (2008-11-01), Luo et al.
patent: 7560251 (2009-07-01), Wang et al.
patent: 2003/0118598 (2003-06-01), Hunt
patent: 2004/0235139 (2004-11-01), Demain et al.
patent: 2006/0228780 (2006-10-01), Luo et al.
patent: 2007/0111288 (2007-05-01), Donovan et al.
patent: WO 94/09115 (1993-10-01), None
patent: WO 96/05222 (1995-06-01), None
patent: WO 98/54296 (1998-05-01), None
patent: WO 01/05997 (2000-07-01), None
patent: WO 01-03665 (2000-10-01), None
patent: WO 01/58472 (2001-02-01), None
patent: WO 2005/035749 (2004-08-01), None
U.S. Appl. No. 11/932,689, filed Oct. 31, 2007, Luo et al.
U.S. Appl. No. 11/932,789, filed Oct. 31, 2007, Luo et al.
U.S. Appl. No. 12/098,896, filed Oct. 7, 2008, Donovan et al.
Bedu-Addo, F., et al. “Use of Biophysical characterization in preformulation development of a heavy-chain fragment of botulinum serotype B: Evaluation of suitable purification process conditions.”Pharmaceutical Research21.8 (2004): 1353:1361.
Bonventre, P.F., et al., Physiology of toxin production byClostridium botulinumtypes A and B, Appl. Microbiol., 1957, vol. 7, pp. 372-374.
Byrne, M., et al. “Purification, potency, and efficacy of the botulinum type A binding domain fromPichia pastorisas a recombinant vaccine candidate.”Infection and Immunity66.10 (1998): 4817-4822.
Chen, F., et al., Biophysical characterization of the stability of the 150-kilodalton botulinum toxin, complex species, Infect Immun, Jun. 1998, 66(6), pp. 2420-2425.
Eds: Coligan, John E., et al., Strategies of Protein Purification and Characterization, Chpt. 1, in Current Protocols in Protein Science, Front Matter, 2003.
Eds: Coligan, John E., et al., Strategies of Protein Purification and Characterization, Peptidases, Chpt. 21, in Current Protocols in Protein Science, Front Matter, 2003.
Gessler, F., et al. “Production and purification ofClostridium botulinumtype C and D neurotoxin.”FEMS Immunology and Medical Microbiology24 (1999): 361-367.
Gimenez, J., et al. “Simplified purification method forClostridium botulinumtype E toxin.”Applied and Environmental Microbiology53.12 (Dec 1987): 2827-2830.
Heenan, C.N., et al., Lehensm.-Wiss. U.-Technol., 35 (2002), pp. 171-176.
Holdeman, L., et al., A study of the nutritional requirements and toxin production ofClostridium botulinumtype F, Canadian Journal of Microbiology, vol. 11, 1965, pp. 1009-1019.
Huhtanen, C.N. “Some observations on a perigo-type inhibition ofClostridium botulinumin a simplified medium.”Journal of Milk and Food Technology38.12 (Dec. 1975): 761-763.
Johnson, E., et al.,Clostridium botulinumand its neurotoxins: a metabolic and cellular perspective, Toxicon, 39 (2001), pp. 1703-1722.
Johnson, S., et al. “Scale-up of the fermentation and purification of the recombinant heavy chain fragment C ofBotulinum neurotoxinserotype F, expressed inPichia pastoris.” Protein Expression and Purification32 (2003): 1-9.
Karasawa, T., et al., A defined growth medium forClostridium difficle, Microbiology (1995), 141, pp. 371-375.
Kohl A., et al., Comparison of the effect of botulinum toxin A (Botox (R)) with the highly-purified neurotoxin (NT 201) in the extensor digitorum brevis muscle test, Mov Disord 2000;15 (Suppl 3):165.
Kozaki, S., et al. “Immunological characterization of papain-induced fragments ofClostridium botulinumtype A neurotoxin and interaction of the fragments with brain synaptosomes.”Infection and Immunity57.9 (1989): 2634-2639.
Lewis, K.H., et al.,Practical media and control measures for highly toxic cultures of Clostridium botulinum type A, Production of Botulinum Toxin, pp. 213-230, (1947).
Li, Y., et al.,Expression and characterization of the heavy chain of tetanus toxin: reconstitution of the fully-recombinant dichain protein in active form, J. Biochem (Tokyo) Jun. 1999, 125(6), pp. 1200-1208.
Ljungdahl, L.G., et al.,Working with Anaerobic Bacteria, Manual of Industrial Microbiology and Biotechnology, Chp. 8, 1986, pp. 84-96.
Miwa, Norinaga, et al., International Journal of Food Microbiology, 49 (1999), pp. 103-106.
Mueller, J.H., et al.,Variable factors influencing the product of tetanus toxin, J. Bacteriol, 1953, 67:271-277.
Naumann M. et al., Botulinum toxin type A in the treatment of focal, axillary and palmar hyperhidrosis and other hyperhidrosis conditions, European J. Neurology 6 (Supp 4) 1999, S111-S115.
Oxoid—Product CM0149—product description, pp. 1-2, ( 2004 ).
Ozutsumi, K., et al.,Rapid, simplified method for production and purification of tetanus toxin, Applied and Environmental Microbiology, Apr. 1985, vol. 49, No. 4, pp. 939-943.
Porfirio, Z., et al.,Specific peptides of casein pancreatic digestion enhance the production of tetanus toxin, J. of Applied Microbiology, 1997, 83, pp. 678-684.
Prabakaran, S., et al. “Botulinum neurotoxin types B and E: Purification, limited proteolysis by endoproteinase Glu-C and Pepsin, and comparison of their indentified cleaved sites relative to the three-dimensional structure of type A neurotoxin.”Toxicon39 (2001): 1515-1531.
Ragona, R.M. et al., Management of Parotid Sialocele with Botulinum Toxin, The Laryngoscope 109:1344-1346:1999.
Schantz, E.J., et al., Lewis, G.E. “Use of Chrystalline type A botulinum toxin in medical research.”Biomedical Aspects of Botulism, Academic Press, Inc., George E. Lewis, Jr., Ed., 1981: 143-150.
Schantz, E.J. et al., Properties and Use of Botulinum Toxin and Other Microbial Neurotoxins in Medicine, Microbiological Reviews, Mar. 1992, vol. 56, No. 1, pp. 80-99.
Schiefer-Ullrich, H., et al.,Comparative studies on physiology and taxonomy of obligatory purinolytic clostridia, Arch Microbiol, 1984, 138, pp. 345-353.
Siegel, L.S.,Fermentation kinetics of botulinum toxin production (types A, B, and E), Biomedical aspects of botulism, New York: Academic Press 1981, pp. 121-128.
Siegel, L.S. “Toxin production byClostridium botulinumtype A under various fermentation conditions.”Applied and Environmental MicrobiologyOct. 1979: 606-611.
Tse, et al.European Journal of Ciochemistry122 (1982): 493-500.
Weatherly, G., et al. “Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography.”Journal of Chromatography A952 (2002): 99-110.
Whitmer, M.E., et al., Development of improved defined media forClostridium botulinumserotypes A, B and E, Applied and Environmental Microbiology, Mar 1988, vol. 54, No. 3, pp. 753-759.

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