Abstract
Full-length human matrix metalloproteinase 3 (prostomelysin or proMMP-3) was produced in Escherichia coli as an intracellular insoluble aggregate that could be solubilized and refolded to yield an activatable proenzyme. The refolded protein was purified to > 95% homogeneity. The recombinant proMMP-3 (re-proMMP-3) could be activated by agents known to stimulate self-catalyzed cleavage of native fibroblast proMMP-3. The N-terminal amino-acid sequence of the re-proMMP-3 and its activation products indicated that they were the same as those obtained with the natural material.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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DNA, Complementary / genetics
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Enzyme Precursors / biosynthesis*
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Enzyme Precursors / genetics
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Enzyme Precursors / isolation & purification
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Escherichia coli / metabolism*
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Fibroblasts
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Humans
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Matrix Metalloproteinase 3
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Metalloendopeptidases / biosynthesis*
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Metalloendopeptidases / genetics
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Metalloendopeptidases / isolation & purification
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Molecular Sequence Data
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Protein Biosynthesis
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RNA, Messenger / biosynthesis
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RNA, Messenger / genetics
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
Substances
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DNA, Complementary
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Enzyme Precursors
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RNA, Messenger
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Recombinant Proteins
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Metalloendopeptidases
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Matrix Metalloproteinase 3