Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants
AA disintegrin-like and metalloproteinase with thrombospondin type-1 motifs-4 (ADAMTS-4) and ADAMTS-5 are zinc-dependent metalloproteinases that are involved in the maintenance of cartilage extracellular matrix (ECM) and are currently considered the major aggrecanases in the development of osteoarth...
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Humana Press
2019
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_version_ | 1826305425292656640 |
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author | Fowkes, MM Lim, NH |
author2 | Apte, SS |
author_facet | Apte, SS Fowkes, MM Lim, NH |
author_sort | Fowkes, MM |
collection | OXFORD |
description | AA disintegrin-like and metalloproteinase with thrombospondin type-1 motifs-4 (ADAMTS-4) and ADAMTS-5 are zinc-dependent metalloproteinases that are involved in the maintenance of cartilage extracellular matrix (ECM) and are currently considered the major aggrecanases in the development of osteoarthritis. In this chapter we describe the establishment and cultivation of cell lines expressing ADAMTS-4,-5 and their domain deletion mutants; the collection of medium containing expressed ADAMTS-4,-5; the subsequent purification of this medium through anti-FLAG affinity chromatography; and the characterization of ADAMTS-4,-5 activity using synthetic Förster resonance energy transfer (FRET) peptide substrates. |
first_indexed | 2024-03-07T06:32:41Z |
format | Book section |
id | oxford-uuid:f68d8f97-12ee-4fe0-a6fb-ff242b767498 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T06:32:41Z |
publishDate | 2019 |
publisher | Humana Press |
record_format | dspace |
spelling | oxford-uuid:f68d8f97-12ee-4fe0-a6fb-ff242b7674982022-03-27T12:35:53ZPurification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutantsBook sectionhttp://purl.org/coar/resource_type/c_3248uuid:f68d8f97-12ee-4fe0-a6fb-ff242b767498EnglishSymplectic Elements at OxfordHumana Press2019Fowkes, MMLim, NHApte, SSAA disintegrin-like and metalloproteinase with thrombospondin type-1 motifs-4 (ADAMTS-4) and ADAMTS-5 are zinc-dependent metalloproteinases that are involved in the maintenance of cartilage extracellular matrix (ECM) and are currently considered the major aggrecanases in the development of osteoarthritis. In this chapter we describe the establishment and cultivation of cell lines expressing ADAMTS-4,-5 and their domain deletion mutants; the collection of medium containing expressed ADAMTS-4,-5; the subsequent purification of this medium through anti-FLAG affinity chromatography; and the characterization of ADAMTS-4,-5 activity using synthetic Förster resonance energy transfer (FRET) peptide substrates. |
spellingShingle | Fowkes, MM Lim, NH Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants |
title | Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants |
title_full | Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants |
title_fullStr | Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants |
title_full_unstemmed | Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants |
title_short | Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants |
title_sort | purification and activity determination of adamts 4 and adamts 5 and their domain deleted mutants |
work_keys_str_mv | AT fowkesmm purificationandactivitydeterminationofadamts4andadamts5andtheirdomaindeletedmutants AT limnh purificationandactivitydeterminationofadamts4andadamts5andtheirdomaindeletedmutants |