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Taylor et al., 1992 - Google Patents

Active papain renatured and processed from insoluble recombinant propapain expressed in Escherichia coli

Taylor et al., 1992

Document ID
12278035852778538586
Author
Taylor M
Pratt K
Revell D
Baker K
Sumner I
Goodenough P
Publication year
Publication venue
Protein Engineering, Design and Selection

External Links

Snippet

For the first time the pro-form of a recombinant cysteine proteinase has been expressed at a high level in Escherichia coli. This inactive precursor can subsequently be processed to yield active enzyme. Sufficient protein can be produced using this system for X-ray …
Continue reading at academic.oup.com (other versions)

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    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • C12N9/6427Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6489Metalloendopeptidases (3.4.24)
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6472Cysteine endopeptidases (3.4.22)
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6402Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
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    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
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    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
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    • C07KPEPTIDES
    • C07K2319/00Fusion polypeptide
    • C07K2319/01Fusion polypeptide containing a localisation/targetting motif
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    • C07KPEPTIDES
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    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
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    • C07K14/81Protease inhibitors
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    • C07K14/811Serine protease (E.C. 3.4.21) inhibitors
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    • C07K14/81Protease inhibitors
    • C07K14/8107Endopeptidase (E.C. 3.4.21-99) inhibitors
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    • C07K14/195Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria

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