Skip to main content

Assay of Matrix Metalloproteinases Against Matrix Substrates

  • Protocol
Matrix Metalloproteinase Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 151))

  • 807 Accesses

Abstract

Mammalian collagenases cleave all three polypeptide chains of the triple helical collagen molecule at a specific site to give characteristic one-quarter and three-quarter fragments. These denature at 37°C becoming susceptible to digestion by less specific proteinases.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 74.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Gisslow M. T. and McBride B. C. (1975) A rapid sensitive collagenase assay. Anal. Biochem. 68, 70–78.

    Article  PubMed  CAS  Google Scholar 

  2. Cawston T. E. and Barrett A. J. (1979) A rapid and reproducible assay for collagenase using [1-14C]acetylated collagen. Anal. Biochem. 99, 340–345.

    Article  PubMed  CAS  Google Scholar 

  3. Terato K., Nagai Y., Kawaninski K., and Shinro Y. (1976) A rapid assay method of collagenase activity using 14C-labeled soluble collagen as substrate. Biochim. Biophys. Acta. 445, 753–762.

    PubMed  CAS  Google Scholar 

  4. Johnson-Wint B. and Gross J. (1980) A quantitative collagen film collagenase assay for large numbers of samples. Anal. Biochem. 104, 175–181.

    Article  PubMed  CAS  Google Scholar 

  5. Lefebvre V. and Vaes G. (1989) Enzymatic evaluation of procollagenase and collagenase inhibitors in crude biological media. Biochim. Biophys. Acta 992, 355–361.

    PubMed  CAS  Google Scholar 

  6. Murphy G., Koklitis P., and Carne A. F. (1989) Dissociation of TIMP from enzyme complexes yields fully active inhibitor. Biochem. J. 261, 1031–1034.

    PubMed  CAS  Google Scholar 

  7. Sellers A., Cartwright E., Murphy G., and Reynolds J. J. (1977) Evidence that latent collagenases are enzyme-inhibitor complexes Biochem. J. 163, 303–307.

    PubMed  CAS  Google Scholar 

  8. Cawston T.E. Galloway W.A., Mercer E., Murphy G., and Reynolds J.J. (1981) Purification of rabbit bone inhibitor of collagenase. Biochem. J. 195, 159–165.

    PubMed  CAS  Google Scholar 

  9. Harris E. D. and Vater C. A. (1982) Vertebrate collagenases. Meth. Enzymol. 82, 423–458.

    Article  PubMed  CAS  Google Scholar 

  10. Cawston T. E. and Murphy G. (1981) Mammalian collagenases. Meth. Enzymol. 80, 711–722.

    Article  PubMed  CAS  Google Scholar 

  11. Dioszegi M., Cannon P., and VanWart H. E. (1995) Vertebrate collagenases. Meth. Enzymol. 248, 413–431 397

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2001 Humana Press Inc.

About this protocol

Cite this protocol

Cawston, T.E., Koshy, P., Rowan, A.D. (2001). Assay of Matrix Metalloproteinases Against Matrix Substrates. In: Clark, I.M. (eds) Matrix Metalloproteinase Protocols. Methods in Molecular Biology™, vol 151. Humana Press. https://doi.org/10.1385/1-59259-046-2:389

Download citation

  • DOI: https://doi.org/10.1385/1-59259-046-2:389

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-733-5

  • Online ISBN: 978-1-59259-046-9

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics