What question did this study set out to answer?

This research aimed to investigate the structural requirements for elastolytic activity in 92-kDa and 72-kDa gelatinases.

The Structural Basis for the Elastolytic Activity of the 92-kDa and 72-kDa Gelatinases

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Randomized trial tests the role of fibronectin type II-like repeats in elastolytic activity of gelatinases, indicating their necessity for function.

This research aimed to investigate the structural requirements for elastolytic activity in 92-kDa and 72-kDa gelatinases.
Expressed the 92-kDa and 72-kDa catalytic domains in Escherichia coli and yeast.
Evaluated elastolytic activity of CD variants with or without fibronectin type II-like repeats.
Conducted binding assays to assess elastin interaction with gelatinase variants.
92 CD/FN demonstrated elastin degradation comparable to full-length 92-kDa gelatinase.
92 and 72 CDs without fibronectin type II-like repeats did not bind elastin.
Recombinant 92-kDa fibronectin type II-like repeats inhibited elastin binding of the 92-kDa gelatinase.

Shipley et al. (1996) studied this question.

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Randomized trial tests the role of fibronectin type II-like repeats in elastolytic activity of gelatinases, indicating their necessity for function.