Abstract
ADAMTS are secreted metalloproteinases implicated in many key biological processes. The 19 different members of this family share an identical domain composition at the level of their amino-terminal portion, whereas the identity and number of the domains forming their carboxy-terminal half are divergent and define distinct ADAMTS subfamilies. Due to their large size, extensive glycosylation, the presence of specific domains, their tendency to form aggregates, their relatively low abundance in tissues and the presence of many disulfide bonds, ADAMTS are very hard to isolate, express, and purify, as either native or recombinant active enzymes. This chapter provides an overview of critical steps to take into account when obtaining these proteases for biochemical and functional investigation.
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Colige, A.C. (2020). Challenges and Solutions for Purification of ADAMTS Proteases: An Overview. In: Apte, S. (eds) ADAMTS Proteases. Methods in Molecular Biology, vol 2043. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9698-8_4
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DOI: https://doi.org/10.1007/978-1-4939-9698-8_4
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