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Machine translation
1. (WO2012104099) PROCESS FOR THE PRODUCTION OF RECOMBINANT TRYPSIN
Latest bibliographic data on file with the International Bureau   

Pub. No.:    WO/2012/104099    International Application No.:    PCT/EP2012/000497
Publication Date: 09.08.2012 International Filing Date: 03.02.2012
IPC:
C12N 9/76 (2006.01)
Applicants: GLUCOMETRIX AG [DE/DE]; Am Mühlenberg 11 14476 Potsdam (DE) (For All Designated States Except US).
KÖNIG, Peter [DE/DE]; (DE) (For US Only)
Inventors: KÖNIG, Peter; (DE)
Agent: BRITTINGER, Matthias; MÜLLER HOFFMANN & PARTNER Innere Wiener Straße 17 81667 München (DE)
Priority Data:
11000899.2 04.02.2011 EP
Title (EN) PROCESS FOR THE PRODUCTION OF RECOMBINANT TRYPSIN
(FR) PROCÉDÉ DE PRODUCTION DE TRYPSINE RECOMBINANTE
Abstract: front page image
(EN)The invention relates to a process for the production of recombinant trypsin and its use for processing of an insulin precursor into insulin. In particular, the invention relates to a process for the production of recombinant trypsin starting from recombinant trypsinogen produced in a prokaryotic host cell. In the process of the invention the recombinant trypsinogen is produced by the host cell in form of inclusion bodies. The trypsinogen contained in the inclusion bodies is purified and subsequently refolded into its native conformation involving formation of disulfide bridges. The refolded trypsinogen is then further processed into active trypsin.
(FR)La présente invention concerne un procédé de production de trypsine recombinante et son utilisation en vue de la transformation d'un précurseur de l'insuline en insuline. L'invention concerne, en particulier, un procédé de production de trypsine recombinante à partir de trypsinogène recombinant produit dans une cellule hôte procaryote. Dans le procédé de l'invention, le trypsinogène recombinant est produit par la cellule hôte sous la forme de corps d'inclusion. Le trypsinogène contenu dans les corps d'inclusion est purifié, puis replié pour retrouver sa conformation native avec formation de ponts disulfure. Le trypsinogène replié subit ensuite une nouvelle transformation pour donner de la trypsine active.
Designated States: AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW.
African Regional Intellectual Property Organization (BW, GH, GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW)
Eurasian Patent Organization (AM, AZ, BY, KG, KZ, MD, RU, TJ, TM)
European Patent Office (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TR)
African Intellectual Property Organization (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, ML, MR, NE, SN, TD, TG).
Publication Language: English (EN)
Filing Language: English (EN)