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1. (DK1907561) CELLELINJER TIL EKSPRESSION AF ENZYM, DER ER ANVENDELIGT I FREMSTILLINGEN AF AMIDEREDE PRODUKTER

Office : Denmark
Application Number: 06785535 Application Date: 23.06.2006
Publication Number: 1907561 Publication Date: 02.12.2013
Grant Number: Grant Date: 02.12.2013
Publication Kind : T3
Prior PCT appl.: Application Number:US2006024687 ; Publication Number: Click to see the data
IPC:
C12P 21/00
C12N 9/00
C12N 9/02
C CHEMISTRY; METALLURGY
12
BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
P
FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
21
Preparation of peptides or proteins
C CHEMISTRY; METALLURGY
12
BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
N
MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
9
Enzymes, e.g. ligases (6.); Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating, or purifying enzymes
C CHEMISTRY; METALLURGY
12
BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
N
MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
9
Enzymes, e.g. ligases (6.); Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating, or purifying enzymes
02
Oxidoreductases (1.), e.g. luciferase
Applicants: Enteris BioPharma, Inc.
Inventors: MILLER, Duncan, A.
Priority Data: 693612 P 24.06.2005 US
Title: (DA) CELLELINJER TIL EKSPRESSION AF ENZYM, DER ER ANVENDELIGT I FREMSTILLINGEN AF AMIDEREDE PRODUKTER
Abstract:
(EN) Cell lines are provided for expressing peptidylglycine alpha-amidating monooxygenase (PAM), or one of its two catalytic domains. High levels of enzyme expression are achieved while utilizing a non-animal source, low protein tissue culture medium. A robust two-step downstream purification results in high enzyme purity. Resulting PAM, or its PHM catalytic domain, is used to catalyze the enzymatic conversion of X-Gly to X-alpha-hydroxy-Gly or X-NH2 (X being a peptide or any chemical compound having a carbonyl group to which a glycine group can be covalently attached). Methods of preparing preferred cell lines are also set forth.
Also published as:
EP1907561JP2008543344JP2011139714JP2012016354CN101287840CA2613471
ES2437068AU2006261909WO/2007/002532