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Drentin et al., 2015 - Google Patents

Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4

Drentin et al., 2015

Document ID
8689775896099607281
Author
Drentin N
Conroy P
Gunzburg M
Pike R
Wijeyewickrema L
Publication year
Publication venue
Molecular Immunology

External Links

Snippet

The interaction between mannose-binding lectin [MBL]-associated serine protease-2 (MASP- 2) and its first substrate, C4 is crucial to the lectin pathway of complement, which is vital for innate host immunity, but also involved in a number of inflammatory diseases. Recent data …
Continue reading at www.sciencedirect.com (other versions)

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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
    • C12N9/6424Serine 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)
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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
    • C12N9/6405Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals not being snakes
    • GPHYSICS
    • G01MEASURING; TESTING
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    • G01N2333/95Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
    • G01N2333/964Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
    • G01N2333/96425Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
    • G01N2333/96427Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
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