Abstract
Publisher Summary The detection and quantification of elastinolytic activity are important considerations when studying model systems designed to evaluate the turnover of mature elastin. The newly synthesized tropoelastin monomer is highly susceptible to degradation by a number of proteinases. However, in this chapter the term elastase is reserved for those proteinases that can directly use fully cross-linked insoluble elastin as a substrate. Furthermore, an elastase must be associated with biological turnover of elastin. It should also be noted that, although most collagenases degrade only collagens, elastases will degrade nonelastin proteins. Therefore, an assay with an elastin substrate will unambiguously define an elastase but may not define the exclusive biological role of the proteinase. The [3H] elastin assay is representative of the more sensitive radioactive elastin assays. It is about threefold more sensitive than the rhodamine assay and takes advantage of the ability of the aldol, isodesmosine, and desmosine cross-links to be reduced and labeled with NaB3H4.
Published Version
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