Abstract
The activated first component of human complement, C1-s, was shown to cleave type I and II collagen and gelatin. The proteolytic activity was heat labile and was inhibited by a monoclonal antibody (M241) which recognized light chain of active human C1-s or by a serine protease inhibitor, DFP, but not by a chelating agent.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Calcium
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Collagen / metabolism*
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Complement C1s / metabolism*
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Enzyme Activation
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Extracellular Matrix / metabolism
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Humans
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Molecular Sequence Data
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Protease Inhibitors / pharmacology
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Serine Endopeptidases / genetics
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Serine Endopeptidases / metabolism
Substances
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Protease Inhibitors
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Collagen
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Serine Endopeptidases
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Complement C1s
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Calcium