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Trypsin-like neutral protease associated with soluble elastin

R P Mecham, J A Foster

    Biochemistry
    |August 23, 1977
    PubMed
    Summary
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    A neutral protease associated with tropoelastin degrades it into small peptides. This enzyme is a serine protease with trypsin-like specificity, inhibited by specific agents.

    Area of Science:

    • Biochemistry
    • Proteomics
    • Enzymology

    Background:

    • Tropoelastin isolation is hindered by an associated neutral protease.
    • This protease degrades tropoelastin into smaller peptides, complicating purification.

    Purpose of the Study:

    • To characterize the substrate and inhibitor specificities of the neutral protease.
    • To identify the enzyme class and catalytic mechanism of the tropoelastin-associated protease.

    Main Methods:

    • Assaying proteolytic activity against casein.
    • Testing esterase activity using specific substrates (N-tosyl-L-arginine methyl ester, tert-butyl-oxycarbonyl-L-alanine p-nitrophenyl ester).
    • Evaluating inhibition by various agents, including phenylmethanesulfonyl fluoride, metal chelators, and specific protease inhibitors.

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    Main Results:

    • The enzyme showed proteolytic activity against casein and esterase activity against N-tosyl-L-arginine methyl ester.
    • No significant elastinolytic activity was observed against treated elastin or maleylated tropoelastin.
    • The protease was inhibited by phenylmethanesulfonyl fluoride, metal chelators, and potent inhibitors of trypsin-like enzymes, including Aprotinin and alpha-1-antitrypsin.

    Conclusions:

    • The tropoelastin-associated enzyme is identified as a neutral serine protease.
    • The enzyme exhibits trypsin-like specificity, explaining its degradation pattern of tropoelastin.